South African Journal of Chemical Engineering 47 (2024) 197–211

Contents lists available at ScienceDirect

South African Journal of Chemical Engineering

journal homepage: www.elsevier.com/locate/sajce

Exploring marine collagen: Sustainable sourcing, extraction methods, and

cosmetic applications
Vicky Prajaputra a, e, f, Nadia Isnaini b, e, f, *, Siti Maryam c, Ernawati Ernawati d, f, Fitri Deliana b,
Haekal Azief Haridhi a, e, Nur Fadli a, e, Sofyatuddin Karina a, e, Sri Agustina a, e,
Nurfadillah Nurfadillah e, g, Iko Imelda Arisa e, g, Lydia Septa Desiyana b, Tedy Kurniawan Bakri b
a
Department of Marine Sciences, Faculty of Marine and Fisheries, Universitas Syiah Kuala, Banda Aceh 23111, Indonesia
b
Department of Pharmacy, Faculty of Mathematics and Natural Sciences, Universitas Syiah Kuala, Banda Aceh 23111, Indonesia
c
Department of Family Welfare Vocational Education, Faculty of Teacher Training and Education, Universitas Syiah Kuala, Banda Aceh 23111, Indonesia
d
Department of Development Economics, Faculty of Economic and Business, Universitas Syiah Kuala, Banda Aceh 23111, Indonesia
e
Research Center for Marine Sciences and Fisheries, Universitas Syiah Kuala, Banda Aceh 23111, Indonesia
f
ARC PUI-PT Nilam Aceh, Universitas Syiah Kuala, Banda Aceh 23111, Indonesia
g
Department of Aquaculture, Faculty of Marine and Fisheries, Universitas Syiah Kuala, Banda Aceh 23111, Indonesia

A R T I C L E I N F O A B S T R A C T

Keywords: The predominant sources of collagen for cosmetic purposes were traditionally derived from bovine and porcine
Collagen products, such as bones, tendons, and connective tissues. However, these sources are gradually declining in
Cosmetics popularity due to their restricted availability, religious constraints, and disease-related concerns. Consequently,
Environmental chemistry
there is an urgent necessity to explore alternative sustainable collagen sources. Marine species offer a promising
Fish
and sustainable supply for alternative collagen sources due to lower risk of disease transmission, freedom from
Marine collagen
Marine sources religious restrictions, biocompatibility, lower molecular weight, lower production costs, and simpler absorption
Marine sciences by the human body. This study objective highlights to explore potential collagen sources from marine resources
(fishes, poriferans, mollusks, crustaceans, echinoderms, and coelenterates) for cosmetic applications. A variety of
marine collagen sources with different extraction techniques will be compared. The study finds that fish by-
products, particularly skins and bones, are becoming a very encouraging sustainable collagen source con­
trasted with other alternatives. They exhibit a significant collagen content, comprising up to 61.26 % of their dry
weight under acid-soluble collagen (ASC) extraction method. Fish skin and bone-derived collagen is mostly
composed of type I collagen and has been proven to possess notable capabilities as an antioxidant, antiaging, and
skin-whitening agent. Therefore, the utilization of marine collagen as a key ingredient in cosmetics promotes
responsible sourcing, encourages eco-friendly practices, and fosters a circular economy by making the most of
underutilized marine materials.

1. Introduction Although natural plant-based compounds are widely utilized in the

Research and the expansion of the cosmetic research business, for
instance, have made significant use of the idea of "going back to nature"
by employing plant extracts that are popular among consumers (Sim and
Nyam, 2021). Natural extracts can be produced using many different
parts of plants, including stalks, blossoms, leaves, fruit, and roots
(Pandurangan et al., 2018). The use of natural extracts for cosmetic
products is gentle on the skin, safe for people with allergies, and gentle
with the earth (Amberg and Fogarassy, 2019; Carvalho et al., 2021).
cosmetics industry, they have several drawbacks that make them less
desirable. These include their slow growth, environmental and cultural
practices that require a more significant investment, and the usage of
arable land becoming a finite resource (Bom et al., 2019).
On the other hand, the oceans have a tremendous diversity of hab­
itats and organisms, from the surface to the depths. Modern aquaculture
techniques also allow for large-scale commercial cultivation of marine
species. Marine resources provide an optimistic and eco-friendly source
of distinctive bioactive substances for the cosmetics sector, and collagen

* Corresponding author.
E-mail address: nadiaisnaini@usk.ac.id (N. Isnaini).

https://doi.org/10.1016/j.sajce.2023.11.006
Received 14 September 2023; Received in revised form 8 November 2023; Accepted 18 November 2023
Available online 21 November 2023
1026-9185/© 2023 The Author(s). Published by Elsevier B.V. on behalf of Institution of Chemical Engineers. This is an open access article under the CC BY-NC-ND
license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
V. Prajaputra et al.
is among the primary elements in this category. Collagen is a complex
macro protein that makes up between 20 and 30 percent of the total
protein found in organisms (Venmathi Maran et al., 2023). It is the
primary structural component of the extracellular matrix in all con­
nective tissues, such as ligaments, bone, skin, cartilage, and tendons, as
well as interstitial tissue (Singh et al., 2023). For many years, collagen
has been a key bioactive ingredient sourced from the bovine and porcine
processing industries for use in cosmetic products (Gaspar-Pintiliescu
et al., 2019).
The use of collagen derived from terrestrial animals, such as
chickens, cattle, and pigs, has found extensive use in the fields of tissue
repair, pharmaceuticals, cosmetics, and alternative medicine. However,
using collagen from these sources poses significant challenges due to its
high cost, potential to induce immune reactions, limited availability,
substantial land requirements, and the risk of infectious disease trans­
mission. Moreover, individuals of Muslim, Hindu, and Jewish faiths,
collectively constituting 38.4 % of the global population, are prohibited
from using such products due to their religious beliefs (Coppola et al.,
2020). Additionally, concerns related to bovine spongiform encepha­
lopathy (BSE), foot-and-mouth disease (FMD), and transmissible spon­
giform encephalopathy (TSE) over the past few decades have made the
use of bovine-derived products a concern for a larger portion of the
population, especially in the United Kingdom and Asia (Tan et al.,
2023). As a result, there is a growing need for alternative sources of
collagen, with marine animals emerging as a sustainable and responsible
choice.
Marine species have recently been considered as prospective sources
of collagen because of the absence of any religious restrictions on its use
and the lack of reports of any potentially transmissible diseases (Raja­
bimashhadi et al., 2023). The utilization of marine collagen not only
addresses environmental concerns but also offers unique properties that
make it a valuable resource for various industries, including cosmetics,
pharmaceuticals, and food, thereby reducing the dependency on
terrestrial collagen sources. According to Amnuaikit et al. (2022),
cosmetic products containing marine collagen have the ability to
enhance facial skin moisture, minimize pores and skin wrinkles, and
significantly brighten the skin when used regularly for a minimum of
two weeks. Marine collagen possesses bioactivities such as antioxidant,
antiaging, moisturizing, and reparative properties in damaged skin
(Gokoglu, 2023). Unfortunately, there is limited research that addresses
and compares the potential sources of collagen from various marine
organisms, including finfish, poriferans (marine sponges), mollusks
(byssus and cephalopods), crustaceans (mantis shrimp), echinoderms
(starfish and sea urchins), and coelenterates (jellyfish). As a result, the
comparative percentages of collagen production from these sources
remain unknown. This study aims to explore sustainable collagen
sources from marine organisms with different extraction methods, and
the potential of marine collagen as an active ingredient in cosmetic
products. The challenge of incorporating marine collagen into the new
field of sustainable blue cosmetics is also discussed.
2. Method for data collection
The literature data, covering the period from 2011 to 2023, were
collected from databases like Science Direct, SCOPUS, Google Scholar,
and Web of Science, where the keywords "collagen" or "marine collagen"
were employed for the extraction and analysis of the literature data.
3. Sources of marine collagen
According to the organisms that provide the raw material, marine
collagen can be split into two distinct groups: vertebrates and in­
vertebrates. The comparison of collagen levels between marine verte­
brate and invertebrate organisms can exhibit significant variations.
Marine vertebrates (finfish) tend to have more complex skeletal systems
and, thus, generally possess a higher collagen content, which is
198
South African Journal of Chemical Engineering 47 (2024) 197–211
prominently found in their bones and skin. On the other hand, in­
vertebrates comprise the vast majority of marine species, and this group
provides an almost endless supply of possible collagen sources. Some
examples of marine invertebrate organisms that contain collagen are
poriferans (marine sponge), molluscs (byssus and cephalopod), crusta­
ceans (mantis shrimp), echinoderms (starfish and sea urchin), and coe­
lenterates (jellyfish). In general, the diversity of marine organisms that
can be used as sources of collagen is shown in Fig. 1 and several collagen
sources from marine organism with different extraction method are
described in Table 1.
3.1. Collagen from finfish
The strategy for processing finfish typically results in the production
of by-products that include heads (9–12 % of the overall fish weight
percentage), bones (9–15 %), skins (1–3 %), intestines (12–18 %), and
scales (5 %); however, the precise composition of these by-products
might vary depending on the size of the fish, the species, the method,
and the technology that was employed. Fish scales, skin, and bones are
identified as finfish by-products having valuable resources, particularly
collagen sources for active ingredients of cosmetic products. Collagen
type I, which may be extracted from these by-products, is more desirable
for cosmetic use since it is biocompatible with human skin. Based on the
previous reports, collagen type I can be extracted from the skins of Alu-
alu (Matarsim et al., 2023), Asian sea bass (Ampitiya et al., 2023),
Round goby (Yemisken et al., 2023), Sole fish (Arumugam et al., 2018),
and Silver-carp (Abdollahi et al., 2018) as well as from the scales of
Parrotfish (Jaziri et al., 2023), bones of Lizardfish (Jaziri et al., 2022),
skins and swim bladder of Yellowfin tuna (Ampitiya et al., 2023;
Kaewdang et al., 2014). Other sources of marine collagen type I with
their specific collagen content (%) are further represented in Table 1.
One of the marine organisms that makes a significant contribution to
the economy is tuna. According to The State of World Fisheries and
Aquaculture published by the FAO, the total yearly capture of tuna
species worldwide was approximately 7.5 million tons in 2018 (FAO,
2018). Indonesia is one of the world’s largest tuna-producing countries,
with the main export commodity for tuna to several countries, such as
Japan, Thailand, Vietnam, and the United States. In 2017, Indonesia
exported a total of 198,131 tons of tuna (Chairany et al., 2023). Tuna is
mainly produced for canning and freezing, typically as a loin or whole
fish. The production process of frozen tuna often discards a significant
number of remaining bones and skin. One of the tuna industries that
produces a significant amount of tuna skin and bones is PT. Yakin Pasifik
Tuna, located in the Lampulo area, Banda Aceh, Indonesia. Typically,
tuna bones and skin are either discarded in landfills or sold at a lower
price for utilization as animal feed. In fact, the waste skin and bone from
the industry that produces tuna loin and fillet can be used as a raw
material for producing collagen and gelatin, providing an additional
benefit. The collagen content in tuna skin is exceptionally high, reaching
as much as 61.26 % (Ampitiya et al., 2023). Despite the fact that tuna
skin and bones can be a good source of collagen, however, vast volumes
of it are still nevertheless wasted.
3.2. Collagen from poriferans
Poriferans, or marine sponges, have a structure similar to the
cancellous architecture of bone tissue and are a major source of collagen.
Sponges are a diverse group of filter-feeding benthic invertebrates found
primarily in saltwater but sometimes in freshwater (approximately 220
species). Marine sponges offer an intriguing and promising biotech­
nology potential that is mostly untapped. In fact, the number of Porifera
species known to date, which is approximately 8500 (Van Soest et al.,
2012), is significantly greater than the number of species investigated
for biomaterials development, which would be a few dozen. Spongin is a
collagenous protein found in the exoskeleton of certain demosponges.
The molecular composition of spongins has not been fully explained
V. Prajaputra et al.
Fig. 1. Marine collagen sources.
because of the great diversity within this family of marine sponges.
According to several previous reported, collagen has been successfully
extracted from several organisms of the Demospongiae class, such as
Ircinia fusca (Pallela et al., 2011), Callyspongiidae (Lin et al., 2011), and
Chondrosia reniformis (Tassara et al., 2023). Researchers have looked at
the possibility of extracting marine collagen from a variety of sponge
species. Among these, Chondrosia reniformis stands out as a potential
source of type I collagen, making it an appealing candidate for use in
both cosmetic and therapeutic contexts (Pozzolini et al., 2018; Tassara
et al., 2023).
3.3. Collagen from molluscs
Mollusca is a phylum that contains many different species, each of
which may be distinguished from the others by the size and shape of
their bodies. Molluscs are recognized for their soft bodies in general, but
most of all, for having a distinctive shell, even though there are a sig­
nificant number of species that do not have one. Zoologists insist that in
order to properly understand molluscs, one must recognize the presence
of a skin with an epidermis and a dermis, each of which is composed of a
single epithelium. In actuality, this organ does not have much of a ca­
pacity for defense, but it is quite active in its interactions with the sur­
rounding environment. Regarding Cephalopods, the dermis and the
outer tunic of the mantle, where the ends of the muscle fibers are found,
are considered to be one and the same structure. There is no evidence to
suggest, as there is for vertebrates, the presence of a papillary dermis
and a reticular dermis that contain the two primary collagen types, I and
III. Multiple research studies have highlighted the potential availability
of type I collagen in byssus (Vallejos et al., 2014) and cephalopods
(Veeruraj et al., 2015), indicating their suitability as potential raw ma­
terial sources for cosmetic products.
3.4. Collagen from crustaceans
The processing of crustacean seafood, most commonly prawns,
shrimp, crabs, and lobsters, results in a significant amount of waste,
consisting of the carapace and the head of the crustacean. About 60 %−
80 % of shrimp, 60 %− 70 % of crab, 60 %− 85 % of lobster, 65 %− 70 %
of crayfish, and 70 %− 75 % of krill are discarded to be waste during
processing (Suresh et al., 2018). The by-product could be separated into
199
South African Journal of Chemical Engineering 47 (2024) 197–211
its component chemicals: 15 %− 40 % chitin, 20 %− 40 % protein, and
20 %− 50 % calcium carbonate (Yan and Chen, 2015). Collagen
extraction from crustaceans, like shrimp and crab shells, faces chal­
lenges when using acid solutions, and the purification process is intri­
cate due to the presence of non-collagenous proteins, rendering it less
efficient. The reason for this limitation is that the structure of collagen
from crustaceans is highly resistant to acid treatment. This resistance to
acid extraction is due to the specific chemical composition and structure
of crustacean collagen. Therefore, enzymatic method is often used to
isolate collagen from crustaceans. These methods are better suited for
breaking down the tough collagen fibers and preserving their integrity.
Enzymatic extraction, in particular, involves the use of specific enzymes
that can break down the collagen without damaging its properties.
Hiransuchalert et al. (2021) have isolated the muscle of several mantis
shrimp, such as M. nepa, H. harpax, E. woodmasoni, and O. cultrifer. The
result showed that the primary collagen found in shrimp muscles re­
sembles type I collagen found in vertebrate muscles. Although the
collagen content percentage is relatively low, ranging from 0.015 % to
0.4878 %, some other crustaceans may display noteworthy collagen
content variations along with differences in the types of collagen they
produce.
3.5. Collagen from echinoderms
Echinoderms, which belong to the phylum Echinodermata, are a
diverse collection of invertebrates that are found only in marine envi­
ronments. There are around 13,000 extinct species of echinoderms,
categorized into 15 groups and 7000 extant species and organized into
five classes: Crinoidea (sea-lilies and featherstars), Ophiuroidea (brit­
tlestars), Holothuroidea (sea-cucumbers), Echinoidea (sea-urchins), and
Asteroidea (starfish). Echinoderm autotomy is a remarkable phenome­
non characterized by the deliberate separation of complex anatomical
structures found in creatures such as brittlestars, featherstars, starfish,
and even sea cucumbers, which can expel their viscera. This process
involves the transection of various tissues and organs, all of which
typically contain collagenous elements critical for maintaining struc­
tural and mechanical integrity. These components, including tendons,
ligaments, and dermal layers, serve functions analogous to their coun­
terparts in other phyla (Wilkie and Candia, 2023).
Starfish are voracious generalist predators that feed on commercial
V. Prajaputra et al. South African Journal of Chemical Engineering 47 (2024) 197–211

Table 1
Collagen from marine sources: classification, part, extraction method, time, yield, collagen type, and method for collagen characterization.
Marine Sources Classification Part Method Time and Collagen Method for Collagen Characterization References
Yield Type

Alu alu (Sphyraena sp.) Vertebrate Skin ASC 72 h; I SDS-PAGE, ATR-FTIR, XRD, DSC, SEM Matarsim et al.,
6.77 % 2023
Asian sea bass (Lates Vertebrate Skin ASC NA; I SDS-PAGE, FTIR, UV-Spectra, XRD, SEM Ampitiya et al.,
calcarifer) 59.31 % 2023
Bigeye tuna (Thunnus Vertebrate Skin ASC 72 h (4 I SDS-PAGE, FTIR, Amino Acid Ahmed et al., 2019
obesus) ◦
C); 13.5 Composition, Zeta Potential
%
PSC 72 h (4 I
◦
C); 16.7
%
Shark (Prionace glauca) Vertebrate Cartillage ASC 48 h (4 I SDS-PAGE, UV-Spectra, DSC, FTIR, Seixas et al., 2020
◦
C); 0.15 Amino Acid Composition, Rheology, CD
%
PSC 48 h (4 I
◦
C); 3.5 %
Ray (Zearaja chilensis and Vertebrate Cartillage ASC 48 h (4 I
Bathyraja brachyurops) ◦
C); 0.92
%
PSC 48 h (4 I
◦
C); 0.50
%
Lizardfish (Saurida tumbil) Vertebrate Bone ASC 72 h (4 I UV-Spectra, ATR-FTIR, SDS-PAGE, XRD, Jaziri et al., 2022
◦
C); 1.73 DSC, Solubility
%
Round goby (Neogobius Vertebrate Skin ASC 48 h (4 I SDS-PAGE, FTIR Yemisken et al.,
melanostomus) ◦
C); 10 % 2023
Seer fish (Scomberomorus Vertebrate Skin ASC NA; I SDS-PAGE, FTIR, UV-Spectra, XRD, SEM Ampitiya et al.,
commerson) 58.21 % 2023
Silver catfish (Pangasius Vertebrate Skin PSC 24 h (4 – Solubility, FTIR, SEM, Rheology Shaik et al., 2023
sp.) ◦
C); 23.6
%
48 h (4 –
◦
C); 26.4
%
Silver catfish (Chrysichthys Vertebrate Skin ASC 24 h; – FTIR, SEM Hukmi and
nigrodigitatus) 4.27 % Sarbon, 2018
PSC 24 h; –
2.27 %
Skipjack tuna (Katsuwonus Vertebrate Tail tendon ASC 72 h; I SDS-PAGE, Viscosity, SEM, FTIR, DSC Chanmangkang
pelamis) 8.67 % et al., 2022
PSC 27 h; I
12.04 %
Head ASC 48 h; I SDS-PAGE, UV-Spectra, Amino Acid Di et al., 2014
2.47 % Analysis, FTIR, Solubility
PSC 48 h; I
5.62 %
Bone ASC 48 h; I
3.57 %
PSC 48 h; I
6.71 %
Giant croaker (Nibea Vertebrate Swim ASC 24 h (4 I SDS-PAGE, FTIR, SEM, Amino Acid Chen et al., 2019
japonica) bladder ◦
C); 11.3 Analysis
%
PSC 8 h (4 ◦ C); I
15.35 %
Bluefin tuna (Thunnus Vertebrate Skin ASC 24 h; 5.4 I SDS-PAGE, Amino Acid Analysis, FTIR, Tanaka et al., 2018
orientalis) % UV-Spectra
Sturgeon fish (Huso huso) Vertebrate Skin ASC 48 h (4 I SDS-PAGE, Amino Acid Analysis, FTIR, Atef et al., 2020
◦
C); 9.98 SEM, DSC
%
PSC 48 h (4 I
◦
C); 9.08
%
Unicornfish (Naso Vertebrate Bone ASC 72 h; 0.4 I SDS-PAGE, UV-Spectra, FTIR, SEM, XRD Fatiroi et al., 2023
reticulatus) %
Yellowfin tuna (Thunnus Vertebrate Skin ASC NA; I FTIR, UV-Spectra, XRD, SEM Ampitiya et al.,
albacares) 61.26 % 2023
Swim ASC 48 h (4 I SDS-PAGE, Amino Acid Analysis, FTIR, Kaewdang et al.,
bladder ◦
C); 1.07 Zeta Potential 2014
%
PSC 48 h (4 I
◦
C); 12.1
%
(continued on next page)

200
V. Prajaputra et al. South African Journal of Chemical Engineering 47 (2024) 197–211

Table 1 (continued )
Marine Sources Classification Part Method Time and Collagen Method for Collagen Characterization References
Yield Type

Parrotfish (Scarus sordidus) Vertebrate Scale ASC 48 h (4 I UV-Spectra, ATR-FTIR, SDS-PAGE, XRD, Jaziri et al., 2023
◦
C); 1.17 DSC, Solubility
%
PSC 48 h (4 I
◦
C); 1 %
Amur sturgeon (Acipenser Vertebrate Cartilage ASC 48 h (4 I SDS-PAGE, FTIR, DSC, SEM, Amino Acid Liang et al., 2014
schrenckii) ◦
C); 27.0 Analysis
%
PSC 48 h (4 II
◦
C); 55.9
%
SSC 48 h (4 I
◦
C); 2.18
%
Megalonibea (Megalonibea Vertebrate Swim ASC 48 h (4 I SDS-PAGE, UV-Spectra, Amino Acid Mo et al., 2023
fusca) bladder ◦
C); 33.4 Analysis, FTIR, XRD, SEM, TEM, Zeta
% Potential, Solubility
PSC 48 h (4 I
◦
C); 84.8
%
Totoaba (Totoaba Vertebrate Swim PSC 24 h (4 I SDS-PAGE, UV-Spectra, Amino Acid Cruz-López et al.,
macdonaldi) bladder ◦
C); 65 % Analysis, FTIR, XRD, Zeta Potential 2023
Blue Shark (Prionace Vertebrate Cartilage PSC 24 h (4 II SDS-PAGE, SEM, UV-Spectra, Amino Pan et al., 2023
glauca) ◦
C); 7.69 Acid Analysis
%
Greenland halibut Vertebrate Skin ASC 96 h (4 I SDS-PAGE, FTIR, Amino Acid Analysis, Martins et al., 2022
(Reinhardtius ◦
C); 3.8 % SEM-EDX, DSC, Rheology
hippoglossoides)
Grass carp Vertebrate Swim PSC 48 h (4 I SDS-PAGE, FTIR, Amino Acid Analysis, Dong and Dai,
(Ctenopharyngodon bladder ◦
C); 38.9 UV-Spectra, DSC, CD Analysis 2022
idella) %
Monkfish (Lophiiformes) PSC 48 h (4 I
◦
C); 10.3
%
Grouper (Epinephelus) PSC 48 h (4 I
◦
C); 18.1
%
Bighead carp (A. nobilis) PSC 48 h (4 I
◦
C); 27.9
%
Catfish (Silurus triostegus) Vertebrate Skin ASC 72 h (4 I SDS-PAGE, FTIR, HPLC, SEM, Solubility, Abbas et al., 2022
◦
C); 2.6 % Viscosity
PSC 72 h (4 I
◦
C); 8.24
%
Bone ASC 72 h (4 I
◦
C); 0.28
%
PSC 72 h (4 I
◦
C); 0.82
%
Muscle ASC 72 h (4 I
◦
C); 0.56
%
PSC 72 h (4 I
◦
C); 0.72
%
Fin ASC 72 h (4 I
◦
C); 0.28
%
PSC 72 h (4 I
◦
C); 0.58
%
Head ASC 72 h (4 I
◦
C); 0.10
%
PSC 72 h (4 I
◦
C); 0.94
%
Dusky grouper (Epinephelus Vertebrate Scale ASC 72 h (8 I SDS-PAGE, SEM, FTIR, XRD, TGA Tziveleka et al.,
marginatus) ◦
C); 0.39 2022
%
PSC 24 h (8 I
◦
C); 1.5 %
(continued on next page)

201
V. Prajaputra et al. South African Journal of Chemical Engineering 47 (2024) 197–211

Table 1 (continued )
Marine Sources Classification Part Method Time and Collagen Method for Collagen Characterization References
Yield Type

Red mullet (Mullus Vertebrate Scale ASC 72 h (8 I

barbatus) ◦
C); 0.6 %
PSC 24 h (8 I
◦
C); 1.0 %
Gilt-head bream (Sparus Vertebrate Scale ASC 72 h (8 I
aurata) ◦
C); 1.1 %
PSC 24 h (8 I
◦
C); 1.6 %
Atlantic salmon (Salmo Vertebrate Scale ASC 72 h (8 I
salar) ◦
C); 0.9 %
PSC 24 h (8 I
◦
C); 2.0 %
Sea Eel (Muraenesox Vertebrate Swim PSC 48 h (24 I SDS-PAGE, FTIR, SEM, UV-Spectra Li et al., 2023a
cinereus) bladder ◦
C); 93.7
%
Sponge (Chondrosia Invertebrate Sponge Enzymatic 72 h (17 IV Amino Acid Analysis, Tassara et al., 2023
reniformis) (poriferans) tissue Digestion ◦
C); 1.96 Glycosaminoglycans Quantification,
% Viscosity, Thermal Stability
72 h (27 IV
◦
C); 3.4 %
Sponge (C. reniformis) Invertebrate Sponge Enzymatic 24 h (37 IV Glycosaminoglycans Quantification, Pozzolini et al.,
(poriferans) tissue Digestion ◦
C); 19 % TEM 2018
Marine sponge (Ircinia Invertebrate Sponge SSC NA; 20.7 I SEM, TEM, SDS-PAGE Pallela et al., 2011
fusca) (poriferans) tissue %
ASC NA; 17.3 I
%
Starfish (Asterina Invertebrate Body wall ASC 72 h (4 I Amino Acid Analysis, UV-Spectra, FTIR, Qi et al., 2016
pectinifera) (Echinoderms) ◦
C); 6.1 % CD Spectra
Starfish (Asterias Invertebrate Body wall UAC 1 h; 3.8 % I Amino Acid Analysis, Zeta Potential, Han et al., 2021
pectinifera) (Echinoderms) TEM
Common starfish (Asterias Invertebrate Body wall ASC+PSC 48 h (4 I UV-Spectra, FTIR, SDS-PAGE, Amino Vate et al., 2023
rubens) (Echinoderms) ◦
C); 1.44 Acid Analysis, SEM, Solubility
%
Sea cucumber Invertebrate Body wall ASC+PSC 72 h (4 I SDS-PAGE, FTIR, UV-Spectra, Amino Li et al., 2020a
(H. cinerascens) (Echinoderms) ◦
C); 72.2 Acid Composition
%
Jellyfish (Rhopilema Invertebrate Jellyfish PSC 72 h (4 I SDS-PAGE, FTIR Felician et al.,
esculentum) (Coelenterate) Filament ◦
C); 4.31 2019
%
Jellyfish (Chrysaora sp.) Invertebrate Tissue PSC 72 h (4 II SDS-PAGE, FTIR, Amino Acid Analysis, Barzideh et al.,
(Coelenterate) (umbrella) ◦
C); 19 % SEM, Zeta Potential, 2014
Jellyfish (Stomolophus Invertebrate Tissue Enzymatic 3 h (45 I Amino Acid Composition Zhuang and Sun,
meleagris) (Coelenterate) Digestion ◦
C); 54.3 2012
%
Jellyfish (Cotylorhiza Invertebrate Tissue PSC 24 h (4 I SDS-PAGE Addad et al., 2011
tuberculata) (Coelenterate) (umbrella) ◦
C); 0.45
%
Tissue (oral PSC 24 h (4 I
arm) ◦
C); 1.94
%
Jellyfish (Catostylus Invertebrate Tissue ASC 72 h (4 I SDS-PAGE, ATR-FTIR, Amino Acid Rastian et al., 2018
mosaicus) (Coelenterate) (umbrella) ◦
C); 1.46 Analysis, AFM, Raman Spectra, CD
% Spectra
Tissue (oral ASC 72 h (4 I
arm) ◦
C); 2.24
%
Jellyfish (Cyanea nozakii) Invertebrate Tissue ASC 72 h (4 I SDS-PAGE, FTIR, Amino Acid Analysis Zhang et al., 2014
(Coelenterate) (umbrella) ◦
C); 13 %
PSC 72 h (4 I
◦
C); 5.5 %
Jellyfish (Rhopilema Invertebrate Tissue ASC 72 h (4 I SDS-PAGE, FTIR, SEM, Amino Acid Cheng et al., 2017
esculentum) (Coelenterate) ◦
C); 0.12 Analysis
%
PSC 24 h (4 I
◦
C); 0.28
%
Byssus of Chilean Mussels Invertebrate Mussels ASC 24 h (80 I SDS-PAGE, Amino Acid Analysis Vallejos et al.,
(Mytilus Chilensis) (Mollusc) ◦
C); 1.8 % 2014
PSC 24 h (80 I
◦
C); 7.6 %
ASC+PSC 24 h (80 I Amino Acid Analysis, Viscosity, Thermal Rodríguez et al.,
◦
C); 6.9 % Stability 2017
Chepalopod Invertebrate Skin pieces ASC 72 h (4 I SDS-PAGE, UV-Spectra, Amino Acid Veeruraj et al.,
(D. singhalensis) (Molluscs) ◦
C); 56.8 Analysis, FTIR 2015
%
(continued on next page)

202
V. Prajaputra et al.
Table 1 (continued )
Marine Sources Classification Part Method
PSC
Mantis Shrimp (Miyakella Invertebrate Muscles PSC
nepa) (Crustacean)
Mantis Shrimp Invertebrate Muscles PSC
(Harpiosquilla harpax) (Crustacean)
Mantis Shrimp Invertebrate Muscles PSC
(Erugosquilla (Crustacean)
woodmasoni)
Mantis Shrimp Invertebrate Muscles PSC
(Odontodactylus cultrifer) (Crustacean)
shellfish (such as mussels, clams, oysters, and other shellfish) and live
coral. Because they are highly reproductive and prey on commercial
shellfish, starfish pose a substantial danger to aquaculture and marine
ecosystems. Starfish have caused varying degrees of disruption in the
coastal and marine ecosystems of Australia, Korea, Japan, Indonesia,
and other countries. A previous study has shown that starfish contain
several different active compounds, one of which is collagen, which has
potential medical applications (Li et al., 2023). Collagen has been suc­
cessfully extracted from several starfish, such as A. pectinifera and A
rubens, with collagen percentages from 1.44 % to 6.1 % (Vate et al.,
2023; Qi et al., 2016; Han et al., 2021). Another study by Li et al.
(2020a) reported the type I collagen extracted from sea cucumber
(H. cinerascens) with a high percentage collagen content up to 72 %.
Therefore, collagen-rich sea cucumber has the potential to be a helpful
collagen sources for the production of pharmaceutical and cosmetic
products, particularly in applications that restrict the use of collagen
derived from bovine and porcine, traditionally recognized as a source of
collagen.
3.6. Collagen from coelenterates
Marine animals belonging to the Phylum Coelenterate have a mouth
equipped with sensory tentacles that make it easier for them to capture
their prey. Their bodies are radially symmetrical and are arranged in a
spiral pattern. The two largest coelenterate groups, Cnidaria and Cte­
nophora, were once classified as subphyla but have since been promoted
to the phylum level. The Phylum Coelenterate includes many diverse
animal groups, such as hydra, comb jellies, true jellies, sea pens, coral
animals, sea anemones, and more. While the vast majority of these
species are marine, we can also find them in brackish and even fresh
water.
A recent investigation delved into the utilization of collagen
extracted from jellyfish, particularly Catastylus mosaicus, as a promising
biomaterial. This study revealed its potential as a viable substitute for
type I collagen, whether in a fibrillar or nonfibrillar state, with appli­
cations in tissue engineering, encompassing both research and industrial
sectors, as outlined by Rastian et al. (2018). Moreover, Felician et al.
(2018) observed that the type I collagen derived from the jellyfish spe­
cies Rhopilema esculentum closely resembles human collagen, making it
suitable for a wide range of medical applications. In addition, peptides
produced from R. esculentum collagen were found to play a role in the
wound-healing processes that occurred in vivo. These peptides increased
the synthesis of chemotactic factors such as β-FGF and TGF-β1.
Furthermore, according to the findings of an in vivo study that compared
bovine sponges and jellyfish as potential prototypes for medical devices,
the collagen in jellyfish has the ability to activate both transcription and
translation, leading to an increase in the production of immunoglobulins
and cytokines. Immunological responses of jellyfish collagen sponges
were confirmed, on par with those elicited by bovine collagen and
gelatin (Widdowson et al., 2018). Lastly, UV protection activity was also
observed in both jellyfish collagen and its hydrolysate, suggesting its
South African Journal of Chemical Engineering 47 (2024) 197–211
Time and Collagen Method for Collagen Characterization References
Yield Type
48 h (4 I
◦
C); 24.6
%
72 h; I SDS-PAGE, FTIR, Solubility Hiransuchalert
0.478 % et al., 2021
72 h; I
0.313 %
72 h; I
0.015 %
72 h; I
0.123 %
potential application in skincare products. As reported by Zhuang and
Sun (2012), collagen peptides isolated from S. meleagris have been
shown to inhibit tyrosinase by increasing glutathione (GSH) levels.
4. Collagen extraction methods
Collagen extraction is a two-step process comprising (a) raw material
preparation and (b) collagen isolation. The initial step involves pre-
treating the raw materials to enhance the purity of the final product
by eliminating contaminants. In this pre-treatment phase, marine by-
products like skin, bone, swim bladder, and scales are first sorted. This
sorting facilitates subsequent tasks such as cleaning, size reduction, and
contaminant removal. Notably, the extracted raw materials are often
rich in lipids, pigments, non-collagenous proteins, and fats (Ampitiya
et al., 2023). Other inorganic minerals like calcium can also be found in
fish skeletons and scales. Demineralization of such bones and scales is
usually accomplished using inorganic compounds like EDTA (Ethyl­
enediaminetetraacetic acid). The removal of the non-collagenous dyes
and fats is accomplished with the use of sodium chloride, sodium hy­
drochloride, and n-butanol.
Collagen extraction methods vary, resulting in four distinct cate­
gories of extracted collagen: acid-soluble collagen (ASC), salt-soluble
collagen (SSC), pepsin-soluble collagen (PSC), and ultrasound-aided
collagen (UAC). The choice of extraction method can substantially in­
fluence both the yield and the physiochemical properties of the extrac­
ted collagen, highlighting the importance of selecting the appropriate
technique for specific applications. The extraction conditions used and
the amino acid composition of collagen extracted from several marine
organisms are summarized in Table 2.
4.1. Acid Solubilization Extraction
Fibrous collagen proteins are less soluble in water than in acid (Cao
et al., 2023). Therefore, collagens are typically extracted using an acidic
medium (typically 0.5 M acetic acid). The collagens thus produced are
known as acid-soluble collagens (ASCs). Fig. 2 shows the schematic
procedure of collagen extraction from fish bone by-products. The
increased repulsion between tropocollagen molecules in an acidic so­
lution has the potential to cause the solubilization of collagen molecules.
Many factors influence collagen production, including the age and type
of animals used, the concentration of acids, the duration of acid treat­
ment, the temperature, and the ratio of acidic solutions to raw materials.
Researchers detailed their experiences using various acids to extract
collagen from the skin of Baltic fish (Gadus morhua). When using acetic
or lactic acid, the largest yield that could be produced was 90 %, but
using citric or hydrochloric acid resulted in 60 % and 18 % yields,
respectively. They also confirmed that the amount of extracted collagen
was raised when an enzymatic treatment (pepsin) was combined with
these acid treatments (Skierka and Sadowska, 2007).
In most cases, the collagen was extracted at a temperature of 4 ◦ C for
a period of time between 24 and 48 h. Several variables, such as
203
 V. Prajaputra et al.
Table 2
Amino acid composition of various marine collagen sources.
Part Method Amino Acid Composition/1000 residues Ref
Gly Pro Glu Ala Asp Arg Cys His Hyp Hyl Ile Leu Lys Met Ser Phe Trp Thr Val Tyr Ala+
Arg

Thunnus obesus skin ASC 227 150 99 99 40 81 1 7 82 9 11 26 33 21 36 21 – 31 22 4 – Ahmed et al.,

PSC 221 148 99 97 42 80 1 7 82 9 13 27 33 20 39 20 – 34 23 5 – 2019
Thunnus obesus bone PSC 215 140 101 92 44 79 2 9 87 10 14 28 39 19 38 20 – 33 24 6 –
Thunnus albacares skin ASC 253 126 112 96 67 78 1 8 80 – 10 24 33 – 38 16 – 34 24 0 – This Study
PSC 251 125 113 92 69 76 1 8 80 – 11 27 32 – 41 15 – 35 24 0 – Ahmed et al.,
2019
Katsuwonus pelamis ASC 337 94 77 125 46 43 – 13 70 – 13 27 23 15 37 18 – 30 25 7 – Ding et al.,
bone 2019
ASC 339.1 104.4 66.7 126.3 46.8 48.3 – 5.3 73.8 4.9 12.7 26 29.5 14.5 33.3 14.3 – 25.2 26 2.9 – Di et al., 2014
PSC 331.8 98.5 78.3 109.5 44.3 51.2 – 2.8 70.3 5.4 21.1 28.3 31.3 – 39.7 23.3 – 29.7 34.4 – –
Sturgeon fish skin ASC 192 133.8 108.8 93 67.2 96 0.1 5.8 77.6 – 15.4 24.8 38 11.4 50.4 25.8 0.7 28.4 22.9 7.9 – Atef et al., 2020
PSC 194 135.5 105.3 94.6 67.6 93.7 0.1 5 80.3 – 16.7 24.7 37.7 11.9 51.7 23.6 1 29 22.3 5.3 – Atef et al., 2020
Thunnus orientalis skin ASC 275.8 104.5 68.1 96.8 39.5 99 – 7.9 64.1 11.6 11.5 21.4 26.3 12.9 34.1 – – 24.9 21.1 3.5 – Tanaka et al.,
2018
C. reniformis tissue PSC 494.8 51.4 72.4 – 74.4 – – – 55.2 21.3 8.2 19 17.1 7.8 47.1 12.6 – 20.8 10.4 8 79.1 Tassara et al.,
2023
Rhopilema esculentum PSC 267.9 72.3 85.8 108.6 68.3 76.9 2.8 5.7 – – 30.5 41.9 51 11.6 44.4 29.6 – 36.5 38 18.3 – Cheng et al.,
tissue 2017
Asterina pectinifera UAC 285.9 102.2 54.1 91.7 29.3 23.2 – 4.8 142 – 7.6 17.4 28.2 23.6 40.1 13.1 – 99 21.2 16.6 – Han et al., 2021
204

tissue
Chondrosia reniformis ED 465.9 55 73.4 – 75.6 – – – 59.8 24 9.9 20.5 20.4 10.4 – 14.1 – 24.3 12.7 9.7 76.8 Tassara et al.,
tissue 2023
Asterina pectinifera ASC 329 104 108 101 57 53 – – 87 – 14 14 12 12 46 7 – 32 16 8 – Qi et al., 2016
body wall
Asterias pectinifera AUC 285.9 102.2 54.1 91.7 29.3 – – 16.6 142 – 7.6 21.2 28.2 23.6 40.1 13.1 16.6 99 21.2 16.6 – Han et al., 2021
body wall
Catostylus mosaicus ASC 309 111 75.5 104.2 57.5 46.9 11 5.3 68.5 6.2 21.7 36.1 25.5 5.8 46.8 17.9 – 26.7 32.7 9.4 – Rastian et al.,
tissue (umbrella) 2018
Catostylus mosaicus 268.6 86.1 107.2 90.2 82.5 51.7 – 5.2 38.2 9.6 30.5 41.8 42.1 11 35 16.1 – 31.6 39.1 13.5 –

South African Journal of Chemical Engineering 47 (2024) 197–211

tissue (oral arm)
Cyanea nozakii tissue ASC 308 80 92 83 79 53 – 6 38 27 23 36 36 5 46 12 – 33 36 7 – Zhang et al.,
(umbrella) 2014
Rhopilema esculentum PSC 267.9 72.3 85.8 – 68.3 76.9 2.8 5.7 – – 30.5 41.9 51 11.6 44.4 29.6 – 36.5 38 18.3 – Cheng et al.,
tissue 2017
Mytilus Chilensis ASC 158 77 123 55 99 89 27 11 53 53 29 36 76 13 43 20 – 37 38 16 – Vallejos et al.,
mussels 2014
PSC 150 70 108 69 107 88 9 29 46 – 28 41 67 7 59 28 – 43 32 17 – Rodríguez
et al., 2017
Nibea japonica swim PSC 327.5 112.4 45 100.1 43.3 47.1 – 8.9 74.8 – 8 15.8 24.3 8.4 25.3 9.2 – 16.8 13.4 1.3 – Chen et al.,
bladder ASC 322.4 107.7 46.6 98.2 43.9 46.9 – 9 73.4 – 8.4 16.2 23.4 9 25.4 9.1 – 16.7 13.5 2 – 2019
Katsuwonus pelamis ASC 336.8 102.9 67.9 126.9 46.1 41.7 0.6 4.4 73.4 4.6 16.8 27.9 30 14.6 31.9 15.9 – 26.8 26.9 3.9 – Di et al., 2014
head PSC 330.2 100.3 77.4 110.8 43.7 50.2 – 3.9 69.8 5.1 24.8 30.9 27.9 4.7 36.8 20.9 – 27.8 32.9 1.9 –
Prionace glauca PSC 353.8 144.1 94.8 117.1 49.0 55.2 – 5.57 74.9 – 12.5 33.3 25.5 0.4 25.3 17.6 – 25.1 21.2 1.86 – Pan et al., 2023
cartilage
V. Prajaputra et al.
Fig. 2. The schematic procedure of collagen extraction from tuna bone by-products.
extraction duration, acetic acid concentration, and temperature, have
successfully been used to extract collagen from seafood by-products.
Skin and scales of fish such as carp (Cyprinus carpio), grass carp (Cte­
nopharyngodon idella), channel catfish (Ictalurus punctatus), chub mack­
erel (Scomber japonicas), Japanese sea bass (Lateolabrax japonicus), horse
mackerel (Trachurus japonicus), and yellowtail snapper were reported to
contain acid-soluble collagen (Kozlowska et al., 2015; Liu et al., 2018;
Tan and Chang, 2018). The findings demonstrate that collagen could be
efficiently extracted from fish processing by-products using acidic so­
lutions, which shows promise for commercial uses.
4.2. Salt solubilization extraction
Since collagen is soluble in salt, saline solutions are used in the
extraction process. Neutral saline solutions, such as sodium chloride,
Tris–HCl, citrates or phosphates, are frequently utilized (Schmidt et al.,
2016). Collagen that has been dissolved in salt water is known as
salt-solubilized collagen. Collagen is extracted using the salt solubili­
zation process from various tissues, including bones, cartilage, skin, and
scales. However, the qualities of the extracted collagen are determined
by the salting-out method used during the salt solubilization extraction
procedure (Hukmi and Sarbon, 2018). Solubilization extractions are
typically followed by acid or enzyme-assisted extractions (Hadfi and
Sarbon, 2019). In order to dissolve type I collagen, a salt concentration
of less than 1.0 M is required, whereas a salt concentration of more than
1.0 M is ideal for precipitating type I collagen. It has been reported that
using NaCl (0.45 M at a ratio of 1:1000 (w/v)) with continuous stirring
for a period of 24 h could extract salt-soluble collagen from the cartilage
and skin of Amur sturgeon (Acipenser schrenckii) (Liang et al., 2014). In
contrast to the procedures of chemical hydrolysis, the extraction of salt
or saline solutions has a greater number of drawbacks. Moreover,
because collagen is less soluble in salts than other proteins, this method
has only seen limited usage for collagen extraction.
4.3. Pepsin solubilization extraction
In most cases, collagen could be extracted without the assistance of
enzymes using a variety of acidic solutions, including acetic acid, lactic
acid, hydrochloric acid, and citric acid. A poor yield was obtained
because the collagens from the various sources could not completely
dissolve in the acidic media (Cao et al., 2023). Pepsin, trypsin, papain,
and other collagenases were employed in conjunction with specific
environmental conditions and pH to extract collagen at a maximal yield;
this technique is known as the enzymatic extraction method. The most
205
South African Journal of Chemical Engineering 47 (2024) 197–211
often used of these enzymes for obtaining collagen from seafood is
pepsin. It is possible to employ pepsin with varying amounts of acetic
acid. Collagens that can be digested by pepsin are known as
pepsin-soluble collagens. Multiple studies have shown that combining
acids with low concentrations of enzymes (pepsin) improves collagen
production (Pal et al., 2015; Jeevithan et al., 2014).
An enzymatic extraction is a viable option for the extraction of
collagen for a number of reasons, including the following: (i) These
enzymes increase the solubilization of collagen in an acetic medium,
which leads to an improvement in the extraction efficiency, (ii) Anti­
genicity of collagen may also be diminished through enzymatic break­
down, (iii) The three-dimensional structure of collagen is unaffected by
the enzymatic process of extraction. Because of these reasons, enzyme-
extracted collagen is finding more uses in the food and pharmaceu­
tical industries (Simpson et al., 2012; Wang et al., 2014).
4.4. Ultrasonication assisted extraction
Protein digestion and extraction are possible through ultra-
sonication, which is an uncomplicated, speedy, risk-free, dependable,
and financially beneficial process. Ultrasonication is often used to in­
crease the activity of enzymes and assist in removing temperature-
sensitive chemicals, all while maintaining a high yield and causing a
low amount of harm. Fig. 3 shows the schematic procedure of collagen
extraction from starfish using ultrasonication, adopted by Han et al.
(2021). Sonication opens up the collagen fibrils, facilitating acid and
enzymatic treatment and significantly reducing the time needed for
extraction compared to conventional methods. According to the findings
of several studies, the configuration of the triple helix was not altered,
and the thermal stability of the extracted collagen was improved as a
result. In addition, the amount of collagen extracted is contingent not
only on the duration of the ultrasonication process but also on the
magnitude of the sound waves.
Kim et al. (2013) found that ultrasonication of collagen extracted
from the skin of sea bass (Lateolabrax japonicus) resulted in a higher
collagen yield than conventional extraction methods (acid or salt soluble
extraction). Furthermore, the ultrasonic method did not affect the in­
dividual components of the collagen molecule. In a study conducted by
Ran and Wang (2014), ultrasonication (at 20 kHz pulsed for 20/20 s)
was the most effective technique for collagen extraction from bovine
tendons. In contrast to ultrasonication, conventional extraction resulted
in a meager yield. Apart from the time and amount of pepsin used in the
ultrasonic extraction process, all other factors were constant. Collagen
extraction by ultrasonication combined with pepsin solubilization
V. Prajaputra et al.
Fig. 3. The schematic procedure of collagen extraction from starfish using ultrasonication (Han et al., 2021a).
contributed to the improved yield (6.2 % in 18 h). However, by con­
ventional extraction, there was only a 2.4 % yield after 48 h. These data
demonstrated that ultrasonication in combination with pepsin increased
collagen efficiency and production without compromising collagen
quality.
5. Marine collagen application in cosmetics
Types I collagen are the most prevalent used in collagen-based cos­
metics due to their moisturizing, anti-wrinkle, anti-aging, wound-
healing, and UV radiation protection qualities (Avila Rodríguez et al.,
2018). Collagen’s ability to form films that lessen transepidermal water
loss (TEWL) is advantageous to both skin and hair (Sionkowska et al.,
2020). This mechanism also converts UV-damaged collagen to elastic
fibers (Salvatore et al., 2020). Collagen extracted from the sea cucumber
(Acaudina molpadioides) has been deemed to have antioxidant properties
due to its ability to prevent H2O2-induced injury in cells of the mono­
cyte/macrophage lineage (RAW264.7 cells) (Li et al., 2020). After
incorporating the suggested ingredients, marine collagen used in bath
cosmetics for children’s significantly reduced the composition’s poten­
tial to irritate skin (Klimaszewska et al., 2019). When added to cosmetics
at various concentrations, collagen extracted from the cartilage of the
Prionace glauca improves the skin’s hydration, texture, and complexion
while reducing oil production and softening fine lines and wrinkles (Lu
et al., 2022). Collagen derived from the sea cucumber’s body wall that
has been treated with pepsin is more effective at absorbing and holding
moisture than glycerol, indicating it may have applications in the cos­
metics industry (Li et al., 2020).
5.1. Antioxidant activity
A component of cosmetic products with antioxidant qualities is hy­
drolyzed collagen. It could penetrate the epidermis more deeply because
the polypeptides are shorter and the peptides are smaller (Sionkowska
et al., 2020). Due to its low molecular weight, hydrolyzed collagen is
better able to fix free radicals by donating an electron or hydrogen.
Hydrolyzed collagen has an antioxidant potential because the peptide
contains hydrophobic amino acids (Aguirre-Cruz et al., 2020). The aging
process could be started by oxidative stress. Increased intracellular
reactive oxygen species levels can cause inflammation, cancerous, car­
diovascular, and age-related diseases (Pozzolini et al., 2018). Marine
collagen, gelatin, and peptides can greatly increase the antioxidant en­
zyme’s activity (Salvatore et al., 2020). For instance, trypsin-derived
C. reniformis collagen hydrolysates have demonstrated potential anti­
oxidant properties (Pozzolini et al., 2018). Since the 2,
206
South African Journal of Chemical Engineering 47 (2024) 197–211
2-Diphenyl-1-picrylhydrazyl (DPPH) test is the most popular way to
gauge ROS-scavenging activity, it was used to gauge antioxidant activ­
ity. These findings demonstrated the potential of C. reniformis collagen
hydrolysates as antioxidant medications.
5.2. Antiaging and skin rejuvenation activity
The dermis and epidermis layers make up human skin. The dermis
layer, which creates the skin’s framework, contains collagen and elastin.
The dermis layer gets nutrients less quickly as we age, causing the skin to
lose its elasticity and become more prone to collagen bundle fragility
(Evans et al., 2021). Because of the normal aging process, the forehead
region, rictus, frown, and the area around the eyes develop wrinkles and
expression lines. Telomere shortening, hormonal changes, mitochon­
drial DNA mutations, and oxidative stress brought on by UV exposure
are all known to accelerate the aging process of the skin. Therefore, eight
minutes of collagen mask use resulted in better skin quality, with instant
benefits for both fine and coarse wrinkles (Mejía-Calvo et al., 2021).
The skin’s hydration, suppleness, density, and wrinkle reduction
could all be enhanced by injecting marine collagen peptides subcuta­
neously or through the epidermis (Ito et al., 2018). Evans et al. (2021)
reported that participants who consumed 10 g of Pangasius hypothala­
mus hydrolyzed collagen powder once daily on an empty stomach for 12
weeks stated the occurrence of improvements in cheek skin hydration
score, elasticity, and reduced wrinkle on both sides of the face. Collagen
is beneficial for anti-aging because it helps restore skin suppleness
(Mitura et al., 2020; Evans et al., 2021). Recent research suggests that
starfish (Asterias pectinifera) collagen peptides outperform fish collagen
in terms of encapsulation effectiveness. Reduced expression of matrix
metalloproteinases (MMPs) in cells that have undergone photoaging as a
consequence of exposure to ultraviolet light has a profound anti-aging
effect. This makes it a promising ingredient for antiaging beauty prod­
ucts (Han et al., 2021). Apart from collagen, carbohydrates derived from
marine organisms also had significant anti-aging benefits, including
antioxidant and immunity-boosting properties.
The antiaging benefits of aquatic plant proteins are remarkable.
There was a significant improvement in skin pigmentation and collagen
breakdown, as well as an increase in skin elasticity when a sunscreen
containing protein 50–70 %, polysaccharide 8–14 %, and the amino acid
was extracted from Spirulina using water (Souza and Campos, 2017).
Mild antiaging effects in vivo were observed for the Spirulina-derived
peptide acetyl amidated peptide I, which decreased matrix metal­
loproteinase (MMP)− 1 and MMP-3 expression in the cytoplasmic matrix
of rodent skin and increased collagen content and the activity of other
antioxidant enzymes (Wang et al., 2015). Among the ethanol extracts
V. Prajaputra et al.
obtained from different processing techniques, the freeze-dried U. rigida
sample had the highest protein content, could significantly reduce
UVB-induced damage to rat cortical astrocytes, and displayed some mild
antiaging effects when applied topically (Zehlila et al., 2017).
5.3. Moisturizing activity
Consumers are becoming increasingly interested in the health ben­
efits of cosmetics like moisturizing, antioxidants, and brightening.
Moisturization is one of the crucial aspects of skincare since it does more
than only prevent skin from drying out by lowering evaporation and
enhancing cellular activity (Kircik, 2016; Razia et al., 2021). Moistur­
izers can either be manufactured chemically or made from natural in­
gredients, with the former being the more popular option. Traditional
moisturizing materials in cosmetics often include polyols like glycerol,
propylene glycol, sorbitol, and polyethylene glycol because of their low
cost and great safety. Furthermore, they could break through the stra­
tum corneum, the skin’s outermost covering. However, polyol mois­
turizers with a high number of hydroxyl groups are highly hygroscopic,
meaning they are sensitive to dampness and cannot hold much water.
When the skin is exposed to a dry, hot, or wet climate, the inner layer of
the skin will absorb a lot of water and distribute it throughout the outer
layer. The epidermis will become abnormally dry and possibly damaged
after a certain amount of time has passed. Consequently, modern
moisturizers become an alternative, typically a blend of traditional and
natural moisturizers at a certain ratio, to counteract this shortcoming,
and the impact is subtle. Plants and animals are the primary sources of
the extracts used to make natural lubricants like polysaccharides, pep­
tides, and other active substances.
Collagen acts as a humectant and a natural film-forming humectant,
binding water to keep the epidermis moist and decreasing evaporation
(Sionkowska et al., 2020). Increasing epidermis moisture and firmness
with collagen (Salvatore et al., 2020). In topical formulations, hydro­
lyzed collagen has a strong moisturizing impact on the stratum corneum
of the skin by raising the hydration level; in just one hour, the skin’s
surface lipids increased from 140 to 180 g. The bigger the collagen
peptide, however, the more difficult it is to penetrate the dermis and
subcutaneous layers. Creams containing collagen derived from algae
and fish were found to be more effective at increasing hydration levels
than creams without collagen when tested over a period of two weeks.
Meanwhile, a firming impact was seen after using a 10 % marine
collagen serum for 20 min (Aguirre-Cruz et al., 2020).
5.4. Skin-whitening activity
The desire to have a fairer and brighter skin tone has been a driving
force behind the incredible growth of the skin-whitening product market
in the Asia-Pacific region over the past few years. In Asian culture,
having a brighter skin tone has traditionally been seen to be a sign of
youthfulness, beauty, and prosperity. This mindset causes a lot of Asian
women to become preoccupied with having beautiful skin and a lighter
skin tone, which in turn contributes to the growing demand for skin-
whitening products. Factors both internal and external to the human
body contribute to the wide range of tones and hues seen in human skin.
Some of these factors include the kind and quantity of melanin in the
skin, heredity, the number of melanosomes, UV exposure, and envi­
ronmental pollution (Naik and Farrukh, 2022; Qian et al., 2020).
Melanin is the primary pigment that is generated by melanocytes in the
epidermis during the process of melanogenesis. Pigmentation, the most
apparent component in determining skin tone, can be divided into
pheomelanin (a red to yellow pigment) and eumelanin (a black to brown
pigment). Melanin is an essential component in the process of shielding
the skin from the potentially damaging effects of ultraviolet radiation
(UVR) and oxidative stress. A previous study has also reported that
melanin could inhibit the development of skin cancer by preventing the
death of cells and protecting cells from the DNA damage caused by
207
South African Journal of Chemical Engineering 47 (2024) 197–211
ultraviolet light (Ghattavi et al., 2022). In spite of the fact that it is
beneficial to the skin’s overall health, the overproduction of melanin can
lead to several significant skin problems, such as freckles, melasma,
solar lentigines, and pigmentation (Qian et al., 2020; Pillaiyar et al.,
2017). Therefore, managing melanogenesis is essential for achieving the
desired level of skin pigmentation.
The enzyme tyrosinase plays the primary function in melanogenesis;
hence, inhibiting its activity is one way to exert control over this process.
The therapy of skin pigmentation has been focused mostly on the
enzyme tyrosinase as its cellular target. In the process of discovering
new tyrosinase inhibitors, it was known that certain functional com­
pounds derived from marine by-products displayed potent inhibitory
actions against tyrosinase. The tyrosinase inhibitory activity of a protein
hydrolysate derived from the shrimp by-product Metapenaeus mono­
ceros was measured to have an IC50 value of 6.13 g/mL. At a concen­
tration of 400 g/mL, the protein hydrolysate made from shrimp by-
product showed a tyrosinase inhibition level of 100 % (Mechri et al.,
2020). Tyrosinase inhibitors obtained from marine by-products have
revealed a considerable potential to cosmeceutical businesses due to
their skin-whitening ability and depigmentation after sunburn, in
addition to their usage in treating hyperpigmentation of human and
animal skin.
Multiple studies, including in vivo and in vitro assays and clinical
trials, have demonstrated that collagen hydrolysates derived from ma­
rine by-products inhibit tyrosinase activity (Hu et al., 2022; Chen et al.,
2018). Milkfish scales collagen peptide was shown to have an
outstanding capacity for moisture absorption (20 %), reduced tyrosinase
activity (IC50= 752.4 g/mL), and production of melanin (IC50= 887.1
g/mL) (Chen et al., 2018). These properties allow it to moisturize the
skin, prevent aging, and whiten the complexion. In a clinical investi­
gation, the serum combined with marine collagen peptide molecules
was shown to have a moisturizing effect; however, only when used
temporarily. The 1 kDa fraction of tuna skin collagen peptide exhibited
antioxidant activity, whereas the 5–10 kDa fraction showed antiaging
(by inhibiting gelatinase and tyrosinase), which was recommended for
application in cosmetics (Park and Jo, 2019).
6. Future perspective of marine collagen in cosmetics
FAO (2022) data show that between 1986 and 2018, global fisheries
and aquaculture production increased by more than 76 million tons,
with marine production accounting for more than 64 % of total pro­
duction. Increases in worldwide fish production have been greatly aided
by recent technological advances in fishing as well as quick improve­
ments in aquaculture (Shavandi et al., 2019). More than 70 % of the
whole marine goes through additional processing before it is marketed,
and around 25 % of the total weight of the yearly marine production
goes to waste due to by-products that are not utilized. Low-quality whole
fish, fish tail and head, fish bone, fish organs, skin, and fillet trims, and
the shells of shellfish and crustaceans are all potential components of the
by-product waste, depending on the species composition. Organic
compounds that are the result of by-products have been recognized as
important resources that have a significant potential for developing
products with additional value (such as cosmeceuticals) and for
resolving some of the issues associated with environmental
contamination.
In recent years, significant research efforts have been dedicated to
the examination of marine by-product resources, including those
derived from various marine resource processing activities. This
increased attention is driven by the recognition of the valuable chem­
icals they contain, along with their potential contributions to human
health. Notably, there has been a considerable number of recent studies
exploring the possible advantages of incorporating marine by-products
into cosmetic applications, as evidenced in Table 3. Marine by-
products need to be well-managed in terms of separation, classifica­
tion, stabilization, and preservation to ensure that the raw materials sent
V. Prajaputra et al. South African Journal of Chemical Engineering 47 (2024) 197–211

Table 3 Lastly, the use of marine collagen sources can indeed pose a risk to
Marine by-products and their functionality for cosmetic products. the marine ecosystem, and it is imperative to take measures to maintain
Source of Utilizable Method of Cosmetic References and balance this delicate environment. One solution to mitigate the
marine by- Products Processing Usefulness impact is the promotion of marine organism by-products. By encour­
products aging the responsible utilization of by-products, we can reduce waste
Codfish and Collagen Acid Absorbs water Alves et al., and the need for additional harvesting. Marine collagen, especially from
Salmon soluble well, reduces 2017; fish by-products, refers to collagen obtained from parts of marine or­
skins collagen dehydration Nasri 2017 ganisms that are typically discarded as waste, such as fish skin, scales,
without
irritating skin
and bones. Instead of being wasted, these by-products can be processed
Greenland Collagen Acid Skin- Martins to extract collagen, reducing the need for additional fishing or har­
halibut soluble moisturizing et al., 2022 vesting solely for collagen production. With rising consumer sensitivity
skin collagen effects to cosmetic products, the use of marine by-products for cosmetics should
Sea bass Collagen Acid Protection and Liu et al.,
be considered. To be generally accepted, cosmetic products’ hygiene,
scales soluble treatment of 2023
collagen skin damaged ecology, allergy, safety, and ethics must be well-organized.
by UV radiation
Scales of L. Collagen Acid Increases skin Song et al., 7. Conclusion
rohita fish soluble hydration; 2023
collagen diminishes
wrinkles
In recent years, there has been a growing recognition and investi­
Scales of Collagen Acid Whitening Zu et al., gation of the potential of marine resources, mainly marine by-products,
Silver peptides soluble agent 2023 as promising collagen sources. Many of these by-products have
Carp collagen demonstrated promising cosmeceutical properties, including skin
Scales of Collagen Pepsin Improve skin Lee et al.,
whitening, antiaging, rejuvenation, and moisturizing effects. Marine
Tilapia hydrolysate soluble hydration and 2023
collagen elasticity; collagen is believed to possess higher bioavailability due to its smaller
reduce particle size and lower molecular weight, facilitating easier absorption
wrinkles. by the body. Additionally, marine collagen is structurally similar to
Mackerel Collagen Pepsin Antiaging agent Herawati human collagen, particularly Type I collagen, which is abundant in the
scad skin hydrolysate soluble et al., 2022
skin. This structural resemblance is thought to enhance its effectiveness
collagen
Skin and Collagen Enzymatic Reducing skin Fu et al., in supporting the production of collagen in the skin, contributing to
bone of peptides hydrolysis water loss and 2022 improved skin elasticity and overall health. However, harnessing marine
bigeye UVB-induced by-products as collagen sources for cosmeceutical use entails careful
tuna skin damage
consideration of various criteria. These include understanding the
Shrimp shell Chitosan Enzymatic Antiaging agent Kong et al.,
oligosaccharide hydrolysis 2018 mechanisms of action of marine processing by-products, selecting
Alaska Collagen Enzymatic Reduced ROS Oh et al., appropriate in vivo or in vitro models for evaluating cosmeceutical
pollock hydrolysate hydrolytes and melanin 2020 products, ensuring hygiene and safety, and assessing economic feasi­
and Olive content bility. Despite the promising attributes of numerous marine processing
flounder
by-products, only a limited percentage of cosmetic compounds derived
skins
A. sturgeon Gelatin Hot water Anti-skin-aging Wang et al., from them have made it to the commercial market. This situation pre­
swim agent 2019 sents both challenges and opportunities for researchers to pioneer
bladder innovative and high-value cosmeceuticals sourced from marine pro­
Silver carp Collagen Enzymatic Anti- Liu et al.,
cessing by-products, thereby contributing to the advancement of sus­
skin peptides hydrolysis photoaging 2019
agent
tainable blue cosmetics.
Silver carp Collagen Enzymatic Reduced ROS Iosageanu
bone peptides hydrolysis and melanin et al., 2021 Data availability
content
Hybrid Collagen Acid UVB-protective Chen et al.,
Data will be made available on request.
Kaluga Hydrolysates soluble agent 2022
and collagen
Japanese Declaration of Competing Interest
sturgeon
The authors declare that there is no conflict of interest.
to industrial processing facilities are of sufficient quality and condition.
Acknowledgments
Despite years of research and development, only a few cosmetic com­
ponents produced from marine by-products have been commercially
The present study was facilitated by Universitas Syiah Kuala and
released (Siahaan et al., 2022). The main reasons for this are the exis­
financially supported by the Ministry of Education, Culture, Research,
tence of cheaper and more reliable production methods, such as chem­
and Technology Republic of Indonesia through the Matching Fund-
ical synthesis or the use of genetically modified microbes, and the
Kedaireka, Grant Program Number 28/E1/PPK/KS.03.00/2023, awar­
isolation of specific compounds, which are typically produced in small
ded to the Research Center for Marine Sciences and Fisheries, Uni­
quantities and have high costs. The market for products utilizing marine
versitas Syiah Kuala. This study was also supported and facilitated by
by-products remains relatively small in comparison to the substantial
PT. Yakin Pasifik Tuna, led by Mr. Almer Hafis Sandy. We express our
annual output of these materials. Consequently, a substantial opportu­
gratitude to three anonymous reviewers and the Editor-in-Chief, Pro­
nity exists to create value-added products from marine by-products. To
fessor Milan Carsky, PhD, for their careful and highly useful reviews that
maximize the potential of extracting bioactive chemicals from marine
have significantly contributed to the improvement of this manuscript.
processing by-products, it is imperative to embrace environmentally
sustainable extraction and processing methods. This approach not only
enhances the value of these resources but also aligns with broader
environmental conservation goals.

208
V. Prajaputra et al. South African Journal of Chemical Engineering 47 (2024) 197–211

References FAO. (2022). The State of World Fisheries and Aquaculture 2022. Towards Blue
Transformation. FAO Rome.
Fatiroi, N.S., Jaziri, A.A., Shapawi, R., Mokhtar, R.A.M., Noordin, W.N.M., Huda, N.,
Abbas, A.A., Shakir, K.A., Walsh, M.K., 2022. Functional properties of collagen extracted
2023. Biochemical and microstructural characteristics of collagen biopolymer from
from catfish (Silurus triostegus) waste. Foods 11 (5), 633.
unicornfish (Naso reticulatus Randall, 2001) bone prepared with various acid types.
Abdollahi, M., Rezaei, M., Jafarpour, A., Undeland, I., 2018. Sequential extraction of gel-
Polymers (Basel) 15 (4), 1054.
forming proteins, collagen and collagen hydrolysate from gutted silver carp
Felician, F.F., Xia, C., Qi, W., Xu, H., 2018. Collagen from marine biological sources and
(Hypophthalmichthys molitrix), a biorefinery approach. Food Chem. 242, 568–578.
medical applications. Chem.Biodivers 15 (5), e1700557.
Addad, S., Exposito, J.Y., Faye, C., Ricard-Blum, S., Lethias, C., 2011. Isolation,
Felician, F.F., Yu, R.H., Li, M.Z., Li, C.J., Chen, H.Q., Jiang, Y., Tang, T., Qi, W.Y., Xu, H.
characterization and biological evaluation of jellyfish collagen for use in biomedical
M., 2019. The wound healing potential of collagen peptides derived from the
applications. Mar. Drugs 9 (6), 967–983.
jellyfish Rhopilema esculentum. Chin. J. Traumatol. 22 (01), 12–20.
Aguirre-Cruz, G., León-López, A., Cruz-Gómez, V., Jiménez-Alvarado, R., Aguirre-
Fu, Y., Li, C., Wang, Q., Gao, R., Cai, X., Wang, S., Zhang, Y., 2022. The protective effect
Álvarez, G., 2020. Collagen hydrolysates for skin protection: oral administration and
of collagen peptides from bigeye tuna (Thunnus obesus) skin and bone to attenuate
topical formulation. Antioxidants 9 (2), 181.
UVB-induced photoaging via MAPK and TGF-β signaling pathways. JFF 93, 105101.
Ahmed, R., Haq, M., Chun, B.S., 2019. Characterization of marine derived collagen
Gaspar-Pintiliescu, A., Stanciuc, A.M., Craciunescu, O., 2019. Natural composite
extracted from the by-products of bigeye tuna (Thunnus obesus). Int. J. Biol.
dressings based on collagen, gelatin and plant bioactive compounds for wound
Macromol. 135, 668–676.
healing: a review. Int. J. Biol. Macromol. 138, 854–865.
Alves, A.L., Marques, A.L., Martins, E., Silva, T.H., Reis, R.L., 2017. Cosmetic potential of
Ghattavi, K., Homaei, A., Kamrani, E., Kim, S.K., 2022. Melanin pigment derived from
marine fish skin collagen. Cosmetics 4 (4), 39.
marine organisms and its industrial applications. Dyes Pigm. 201, 110214.
Amberg, N., Fogarassy, C., 2019. Green consumer behavior in the cosmetics market.
Gokoglu, N., 2023. Value addition to seafood processing waste by using enzymes. Value-
Resources 8 (3), 137.
Addition in Agri-food Industry Waste Through Enzyme Technology. Academic Press,
Amnuaikit, T., Shankar, R., Benjakul, S., 2022. Hydrolyzed fish collagen serum from by-
pp. 95–106.
product of food industry: cosmetic product formulation and facial skin evaluation.
Hadfi, N.H., Sarbon, N.M., 2019. Physicochemical properties of silver catfish (Pangasius
Sustainability 14 (24), 16553.
sp.) skin collagen as influenced by acetic acid concentration. Food Res. 3 (6),
Ampitiya, A.G.D.M., Gonapinuwala, S.T., Fernando, C.A.N., De Croos, M.D.S.T., 2023.
783–790.
Extraction and characterisation of type I collagen from the skin offcuts generated at
Han, S.B., Won, B., Yang, S.C., Kim, D.H., 2021a. Asterias pectinifera derived collagen
the commercial fish processing centres. J. Food Sci. Technol. 60 (2), 484–493.
peptide-encapsulating elastic nanoliposomes for the cosmetic application. J. Ind.
Arumugam, G.K.S., Sharma, D., Balakrishnan, R.M., Ettiyappan, J.B.P., 2018. Extraction,
Eng. Chem. 98, 289–297.
optimization and characterization of collagen from sole fish skin. Sustain. Chem.
Han, Y., Guo, Y., Cui, S.W., Li, H., Shan, Y., Wang, H., 2021b. Purple sweet potato extract
Pharm. 9, 19–26.
extends lifespan by activating autophagy pathway in male Drosophila melanogaster.
Atef, M., Ojagh, S.M., Latifi, A.M., Esmaeili, M., Udenigwe, C.C., 2020. Biochemical and
Exp. Gerontol. 144, 111190.
structural characterization of sturgeon fish skin collagen (Huso huso). J. Food
Herawati, E., Akhsanitaqwim, Y., Agnesia, P., Listyawati, S., Pangastuti, A.,
Biochem. 44 (8), e13256.
Ratriyanto, A., 2022. In vitro antioxidant and antiaging activities of collagen and its
Avila Rodríguez, M.I., Rodríguez Barroso, L.G., Sánchez, M.L, 2018. Collagen: a review
hydrolysate from mackerel scad skin (Decapterus macarellus). Mar. Drugs 20 (8),
on its sources and potential cosmetic applications. J. Cosmet. Dermatol. 17 (1),
516.
20–26.
Hiransuchalert, R., Oonwiset, N., Imarom, Y., Chindudsadeegul, P., Laongmanee, P.,
Barzideh, Z., Latiff, A.A., Gan, C.Y., Benjakul, S., Karim, A.A., 2014. Isolation and
Arnupapboon, S., 2021. Extraction and characterization of pepsin-soluble collagen
characterisation of collagen from the ribbon jellyfish (Chrysaora sp.). Int. J. Food Sci.
from different mantis shrimp species. Fish Aquatic Sci. 24 (12), 406–414.
Technol. 49 (6), 1490–1499.
Hu, Z.Z., Sha, X.M., Zhang, L., Zha, M.J., Tu, Z.C., 2022. From fish scale gelatin to
Bom, S., Jorge, J., Ribeiro, H.M., Marto, J.O.A.N.A., 2019. A step forward on
tyrosinase inhibitor: a novel peptides screening approach application. Front. Nutr. 9.
sustainability in the cosmetics industry: a review. J. Clean. Prod. 225, 270–290.
Hukmi, N.M.M., Sarbon, N.M., 2018. Isolation and characterization of acid soluble
Cao, C., Wang, H., Zhang, J., Kan, H., Liu, Y., Guo, L., Tong, H., Wu, Y., Ge, C., 2023.
collagen (ASC) and pepsin soluble collagen (PSC) extracted from silver catfish
Effects of extraction methods on the characteristics, physicochemical properties and
(Pangasius sp.) skin. Int. Food Res. J. 25 (6).
sensory quality of collagen from Spent-Hens bones. Foods 12 (1), 202.
Iosageanu, A.N.D.R.E.E.A., Oancea, A.N.C.A., Ilie, DA.N.I.E.L.A., Anton, E.D., &
Carvalho, M.J., Oliveira, A.L., Pedrosa, S.S., Pintado, M., Madureira, A.R., 2021.
Craciunescu, O. (2021). The effect of fish bone bioactive peptides on the wound
Potential of sugarcane extracts as cosmetic and skincare ingredients. Ind. Crops Prod.
healing process: an in vitro study on keratinocytes. Rom. Biotechnol. Lett., 26,
169, 113625.
2692–2699.
Chairany, N., Padhil, A., Mail, A., Rauf, N., 2023. Risk analysis of supply chain food loss
Ito, N., Seki, S., Ueda, F., 2018. Effects of composite supplement containing collagen
on fishery products using failure mode effect and supply chain operation reference
peptide and ornithine on skin conditions and plasma IGF-1 levels—A randomized,
model. Ind. Eng. Manag. 22 (1), 31–42.
double-blind, placebo-controlled trial. Mar. Drugs 16 (12), 482.
Chanmangkang, S., Wangtueai, S., Pansawat, N., Tepwong, P., Panya, A., Maneerote, J.,
Jaziri, A.A., Shapawi, R., Mokhtar, R.A.M., Noordin, W.N.M., Huda, N., 2023. Extraction
2022. Characteristics and properties of acid-and pepsin-solubilized collagens from
and characterization of type I collagen from parrotfish (Scarus sordidus Forsskål,
the tail tendon of Skipjack Tuna (Katsuwonus pelamis). Polymers (Basel) 14 (23),
1775) scale solubilized with the aid of acetic acid and pepsin. Int. J. Biomater. 2023.
5329.
Jaziri, A.A., Shapawi, R., Mokhtar, R.A.M., Noordin, W.N.M., Huda, N., 2022.
Chen, B., Yu, L., Wu, J., Qiao, K., Cui, L., Qu, H., Su, Y., Cai, S., Liu, Z., Wang, Q., 2022.
Biochemical analysis of collagens from the bone of lizardfish (Saurida tumbil Bloch,
Effects of collagen hydrolysate from large hybrid sturgeon on mitigating ultraviolet
1795) extracted with different acids. PeerJ 10, e13103.
b-induced photodamage. Front. bioeng. biotechnol. 10.
Jeevithan, E., Wu, W., Nanping, W., Lan, H., Bao, B., 2014. Isolation, purification and
Chen, Y.P., Wu, H.T., Wang, G.H., Liang, C.H., 2018. Improvement of skin condition on
characterization of pepsin soluble collagen isolated from silvertip shark
skin moisture and anti-melanogenesis by collagen peptides from milkfish (Chanos
(Carcharhinus albimarginatus) skeletal and head bone. Process. Biochem. 49 (10),
chanos) scales. IOP Conf. Ser. Mater. Sci. Eng. 382 (2), 022067.
1767–1777.
Chen, Y., Jin, H., Yang, F., Jin, S., Liu, C., Zhang, L., Huang, J., Wang, S., Yan, Z., Cai, X.,
Kaewdang, O., Benjakul, S., Kaewmanee, T., Kishimura, H., 2014. Characteristics of
Zhao, R., Yu, F., Yang, Z., Ding, G., Tang, Y., 2019. Physicochemical, antioxidant
collagens from the swim bladders of yellowfin tuna (Thunnus albacares). Food Chem
properties of giant croaker (Nibea japonica) swim bladders collagen and wound
155, 264–270.
healing evaluation. Int. J. Biol. Macromol. 138, 483–491.
Kim, H.K., Kim, Y.H., Park, H.J., Lee, N.H., 2013. Application of ultrasonic treatment to
Cheng, X., Shao, Z., Li, C., Yu, L., Raja, M.A., Liu, C., 2017. Isolation, characterization
extraction of collagen from the skins of sea bass Lateolabrax japonicus. Fish. sci. 79,
and evaluation of collagen from jellyfish Rhopilema esculentum Kishinouye for use in
849–856.
hemostatic applications. PLoS ONE 12 (1), e0169731.
Kircik, L.H., 2016. Evidence-based skincare: the importance of offering moisturization,
Coppola, D., Oliviero, M., Vitale, G.A., Lauritano, C., D’Ambra, I., Iannace, S., de
relief, and protection in common skin disorders. J. Drugs Dermatol. 15 (11), s76.
Pascale, D., 2020. Marine collagen from alternative and sustainable sources:
Klimaszewska, E., Seweryn, A., Ogorzałek, M., Nizioł-Łukaszewska, Z., Wasilewski, T.,
extraction, processing and applications. Mar. Drugs 18 (4), 214.
2019. Reduction of irritation potential caused by anionic surfactants in the use of
Cruz-López, H., Rodríguez-Morales, S., Enríquez-Paredes, L.M., Villarreal-Gómez, L.J.,
various forms of collagen derived from marine sources in cosmetics for children. TSD
True, C., Olivera-Castillo, L., Fernández-Velasco, D.A., López, L.M., 2023. Swim
56 (3), 180–187.
bladder of farmed Totoaba macdonaldi: a source of value-added collagen. Mar. Drugs
Kong, S.Z., Li, J.C., Li, S.D., Liao, M.N., Li, C.P., Zheng, P.J., Guo, M.H., Tan, W.X.,
21 (3), 173.
Zheng, Z.H., Hu, Z., 2018. Anti-aging effect of chitosan oligosaccharide on D-
Di, Y.U., Chang-Feng, C.H.I., Bin, W.A.N.G., Guo-Fang, D.I.N.G., Zhong-Rui, L.I., 2014.
galactose-induced subacute aging in mice. Mar. Drugs 16 (6), 181.
Characterization of acid-and pepsin-soluble collagens from spines and skulls of
Kozlowska, J., Sionkowska, A., Skopinska-Wisniewska, J., Piechowicz, K., 2015.
skipjack tuna (Katsuwonus pelamis). CJNM 12 (9), 712–720.
Northern pike (Esox lucius) collagen: extraction, characterization and potential
Ding, D., Du, B., Zhang, C., Zaman, F., Huang, Y., 2019. Isolation and identification of an
application. Int. J. Biol. Macromol. 81, 220–227.
antioxidant collagen peptide from skipjack tuna (Katsuwonus pelamis) bone. RSC
Lee, M., Kim, E., Ahn, H., Son, S., Lee, H., 2023. Oral intake of collagen peptide NS
Adv. 9 (46), 27032–27041.
improves hydration, elasticity, desquamation, and wrinkling in human skin: a
Dong, Y., Dai, Z., 2022. Physicochemical, structural and antioxidant properties of
randomized, double-blinded, placebo-controlled study. Food Funct. 14 (7),
collagens from the swim bladder of four fish species. Mar. Drugs 20 (9), 550.
3196–3207.
Evans, M., Lewis, E.D., Zakaria, N., Pelipyagina, T., Guthrie, N., 2021. A randomized,
Li, P.H., Lu, W.C., Chan, Y.J., Ko, W.C., Jung, C.C., Le Huynh, D.T., Ji, Y.X, 2020a.
triple-blind, placebo-controlled, parallel study to evaluate the efficacy of a
Extraction and characterization of collagen from sea cucumber (Holothuria
freshwater marine collagen on skin wrinkles and elasticity. J. Cosmet. Dermatol. 20
cinerascens) and its potential application in moisturizing cosmetics. Aquaculture 515,
(3), 825–834.
734590.
FAO. (2018). The state of world fisheries and Aquaculture—2019 (SOFIA).

209
V. Prajaputra et al.
Li, H., Tian, J., Cao, H., Tang, Y., Huang, F., Yang, Z., 2023a. Preparation of enzyme-
soluble swim bladder collagen from Sea Eel (Muraenesox cinereus) and evaluation its
wound healing capacity. Mar. Drugs 21 (10), 525.
Li, L., Yu, Y., Wu, W., Wang, P., 2023b. Extraction, characterization and osteogenic
activity of a Type I collagen from starfish (Asterias amurensis). Mar. Drugs 21 (5),
274.
Li, W., Wang, Y., Wei, H., Zhang, Y., Guo, Z., Qiu, Y., Wen, L., Xie, Z., 2020b. Structural
characterization of Lanzhou lily (Lilium davidii var. unicolor) polysaccharides and
determination of their associated antioxidant activity. J. Sci. Food Agric. 100 (15),
5603–5616.
Liang, Q., Wang, L., Sun, W., Wang, Z., Xu, J., Ma, H., 2014. Isolation and
characterization of collagen from the cartilage of Amur sturgeon (Acipenser
schrenckii). Process Biochem 49 (2), 318–323.
Lin, Z., Solomon, K.L., Zhang, X., Pavlos, N.J., Abel, T., Willers, C., Dai, K., Xu, J.,
Zheng, Q., Zheng, M., 2011. In vitro evaluation of natural marine sponge collagen as
a scaffold for bone tissue engineering. Int. J. Biol. Sci. 7 (7), 968–977.
Liu, Y., Ma, D., Wang, Y., Qin, W., 2018. A comparative study of the properties and self-
aggregation behavior of collagens from the scales and skin of grass carp
(Ctenopharyngodon idella). Int. J. Biol. Macromol. 106, 516–522.
Liu, Y., Qin, D., Wang, H., Zhu, Y., Bi, S., Liu, Y., Cheng, X., Chen, X., 2023. Effect and
mechanism of fish scale extract natural hydrogel on skin protection and cell damage
repair after UV irradiation. Colloids Surf. B. 225, 113281.
Liu, Z., Li, Y., Song, H., He, J., Li, G., Zheng, Y., Li, B., 2019. Collagen peptides promote
photoaging skin cell repair by activating the TGF-β/Smad pathway and depressing
collagen degradation. Food Funct. 10 (9), 6121–6134.
Lu, W.C., Chiu, C.S., Chan, Y.J., Guo, T.P., Lin, C.C., Wang, P.C., Lin, P.Y., Mulio, A.T.,
Li, P.H., 2022. An in vivo study to evaluate the efficacy of blue shark (Prionace
glauca) cartilage collagen as a cosmetic. Mar. Drugs 20 (10), 633.
Martins, E., Fernandes, R., Alves, A.L., Sousa, R.O., Reis, R.L., Silva, T.H., 2022. Skin by-
products of Reinhardtius hippoglossoides (Greenland Halibut) as ecosustainable source
of marine collagen. Appl. Sci. 12 (21), 11282.
Matarsim, N.N., Jaziri, A.A., Shapawi, R., Mokhtar, R.A.M., Noordin, W.N.M., Huda, N.,
2023. Type I collagen from the skin of Barracuda (Sphyraena sp.) prepared with
different organic acids: biochemical, microstructural and functional properties.
J. Funct. Biomater. 14 (2), 87.
Mechri, S., Sellem, I., Bouacem, K., Jabeur, F., Chamkha, M., Hacene, H., Bouanane-
Darenfed, A., Jaouadi, B., 2020. Antioxidant and enzyme inhibitory activities of
Metapenaeus monoceros by-product hydrolysates elaborated by purified alkaline
proteases. Waste Biomass Valoriz. 11, 6741–6755.
Mejía-Calvo, I., López-Juárez, L.E., Vázquez-Leyva, S., López-Morales, C.A., Montoya-
Escutia, D., Merlos Rivera, P.G., Herbert-Pucheta, J.E., Zepeda-Vallejo, L.G., Velasco-
Velázquez, M., Pavón, L., Medina-Rivero, E., 2021. Quality attributes of partially
hydrolyzed collagen in a liquid formulation used for skin care. J. Cosmet. Dermatol.
20 (1), 150–158.
Mitura, S., Sionkowska, A., Jaiswal, A., 2020. Biopolymers for hydrogels in cosmetics.
J. Mater. Sci.: Mater. Med. 31, 1–14.
Mo, C., Wang, Q., Li, G., Dong, W., Liang, F., Wu, C., Wang, Z., Wang, Y., 2023.
Extraction and characterization of pepsin-and acid-soluble collagen from the swim
bladders of Megalonibea fusca. Mar. Drugs 21 (3), 159.
Naik, P.P., Farrukh, S.N., 2022. Influence of ethnicities and skin color variations in
different populations: a review. Skin Pharmacol. Physiol. 35 (2), 65–76.
Nasri, M., 2017. Protein hydrolysates and biopeptides: production, biological activities,
and applications in foods and health benefits. A review. Adv. Food Nutr. 81,
109–159.
Oh, J.Y., Lee, H.G., Je, J.G., Wang, L., Kim, H.S., Jeon, Y.J., 2020. Evaluation of
cosmeceutical properties of fish skin by-product hydrolysates collected during surimi
manufacturing process. J. Fish Aquat. Sci. 53 (3), 297–307.
Pal, G.K., Nidheesh, T., Suresh, P.V., 2015. Comparative study on characteristics and in
vitro fibril formation ability of acid and pepsin soluble collagen from the skin of catla
(Catla catla) and rohu (Labeo rohita). Food Res. Int. 76, 804–812.
Pallela, R., Bojja, S., Janapala, V.R., 2011. Biochemical and biophysical characterization
of collagens of marine sponge, Ircinia fusca (Porifera: demospongiae: irciniidae). Int.
J. Biol. Macromol. 49 (1), 85–92.
Pan, Z., Ge, B., Wei, M., Elango, J., Wu, W., 2023. Isolation and biochemical properties of
type II collagen from blue shark (Prionace glauca) cartilage. Mar. Drugs 21 (5), 260.
Pandurangan, P., Sahadeven, M., Sunkar, S., Dhana, S.K.N.M., 2018. Comparative
analysis of biochemical compounds of leaf, flower and fruit of Couroupita guianensis
and synthesis of silver nanoparticles. Pharmacogn. J. 10 (2).
Park, S.H., Jo, Y.J., 2019. Static hydrothermal processing and fractionation for
production of a collagen peptide with anti-oxidative and anti-aging properties.
Process Biochem 83, 176–182.
Pillaiyar, T., Manickam, M., Jung, S.H., 2017. Recent development of signaling pathways
inhibitors of melanogenesis. Cell. Signal. 40, 99–115.
Pozzolini, M., Scarfì, S., Gallus, L., Castellano, M., Vicini, S., Cortese, K., Gagliani, M.C.,
Bertolino, M., Costa, G., Giovine, M., 2018. Production, characterization and
biocompatibility evaluation of collagen membranes derived from marine sponge
Chondrosia reniformis Nardo, 1847. Mar. Drugs 16 (4), 111.
Qi, H., Li, N., Zhao, X., Xu, Z., Qi, L., 2016. Physicochemical properties and the radical
scavenging capacities of pepsin-solubilized collagen from the body wall of starfish
(Asterina pectinifera). J. Aquat. Food Prod. 26 (4), 376–389.
Qian, W., Liu, W., Zhu, D., Cao, Y., Tang, A., Gong, G., Su, H., 2020. Natural
skinwhitening compounds for the treatment of melanogenesis. Exp.Ther. Med. 20
(1), 173–185.
Rajabimashhadi, Z., Gallo, N., Salvatore, L., Lionetto, F., 2023. Collagen derived from
fish industry waste: progresses and challenges. Polymers (Basel) 15 (3), 544.
210
South African Journal of Chemical Engineering 47 (2024) 197–211
Ran, X.G., Wang, L.Y., 2014. Use of ultrasonic and pepsin treatment in tandem for
collagen extraction from meat industry by-products. J. Sci. Food Agric. 94 (3),
585–590.
Rastian, Z., Pütz, S., Wang, Y., Kumar, S., Fleissner, F., Weidner, T., Parekh, S.H., 2018.
Type I collagen from jellyfish Catostylus mosaicus for biomaterial applications. ACS
Biomater. Sci. Eng. 4 (6), 2115–2125.
Razia, S., Park, H., Shin, E., Shim, K.S., Cho, E., Kim, S.Y., 2021. Effects of Aloe vera
flower extract and its active constituent isoorientin on skin moisturization via
regulating involucrin expression: in vitro and molecular docking studies. Molecules
26 (9), 2626.
Rodríguez, F., Morán, L., González, G., Troncoso, E., Zúñiga, R.N., 2017. Collagen
extraction from mussel byssus: a new marine collagen source with physicochemical
properties of industrial interest. J. Food Sci. Technol. 54, 1228–1238.
Salvatore, L., Gallo, N., Natali, M.L., Campa, L., Lunetti, P., Madaghiele, M., Blasi, F.S.,
Corallo, A., Capobianco, L., Sannino, A., 2020. Marine collagen and its derivatives:
versatile and sustainable bio-resources for healthcare. Mater. Sci. Eng.: C 113,
110963.
Seixas, M.J., Martins, E., Reis, R.L., Silva, T.H., 2020. Extraction and characterization of
collagen from elasmobranch byproducts for potential biomaterial use. Mar. drugs 18
(12), 617.
Schmidt, M.M., Dornelles, R.C.P., Mello, R.O., Kubota, E.H., Mazutti, M.A., Kempka, A.
P., Demiate, I.M., 2016. Collagen extraction process. Int. Food Res. J. 23 (3), 913.
Shaik, M.I., Md Nor, I.N., Sarbon, N.M., 2023. Effect of extraction time on the
extractability and physicochemical properties of pepsin—soluble collagen (PCS)
from the skin of silver catfish (Pangasius sp. Gels 9 (4), 300.
Shavandi, A., Hou, Y., Carne, A., McConnell, M., Bekhit, A.E.D.A., 2019. Marine waste
utilization as a source of functional and health compounds. Adv. Food Nutr. 87,
187–254.
Siahaan, E.A., Agusman, Pangestuti R., Shin, K.H., Kim, S.K, 2022. Potential cosmetic
active ingredients derived from marine by-products. Mar. Drugs 20 (12), 734.
Sim, Y.Y., Nyam, K.L., 2021. Application of Hibiscus cannabinus L. (kenaf) leaves extract
as skin whitening and anti-aging agents in natural cosmetic prototype. Ind Crops
Prod. 167, 113491.
Simpson, B.K., Nollet, L.M., Toldrá, F., Benjakul, S., Paliyath, G., Hui, Y.H., 2012. Food
Biochemistry and Food Processing. John Wiley & Sons.
Singh, D., Rai, V., Agrawal, D.K., 2023. Regulation of collagen I and collagen III in tissue
injury and regeneration. Cardiol. Cardiovasc. Med. 7 (1), 5.
Sionkowska, A., Adamiak, K., Musiał, K., Gadomska, M., 2020. Collagen based materials
in cosmetic applications: a review. Materials (Basel) 13 (19), 4217.
Skierka, E., Sadowska, M., 2007. The influence of different acids and pepsin on the
extractability of collagen from the skin of Baltic cod (Gadus morhua). Food Chem 105
(3), 1302–1306.
Song, H.H., Hong, K.B., Kim, S., Kim, B.Y., Shik, S.H., Suh, H.J., Ahn, Y., 2023. Effects of
fish collagen on hairless mice skin photoaging induced by ultraviolet irradiation via
regulation of the TGF-β signaling pathway: anti-photoaging effect of fish collagen in
UVB-induced hairless mice. JFF 105, 105554.
Souza, C., Campos, P.M.M, 2017. Development and photoprotective effect of a sunscreen
containing the antioxidants Spirulina and dimethylmethoxy chromanol on sun-
induced skin damage. Eur. J. Pharm. Sci. 104, 52–64.
Suresh, P.V., Kudre, T.G., Johny, L.C., 2018. Sustainable valorization of seafood
processing by-product/discard. Waste wealth 111–139.
Tan, A., Salman, M., Wagner, B., McCluskey, B., 2023. The role of animal health
components in a biosurveillance system: concept and demonstration. Agriculture 13
(2), 457.
Tan, Y., Chang, S.K., 2018. Isolation and characterization of collagen extracted from
channel catfish (Ictalurus punctatus) skin. Food Chem 242, 147–155.
Tanaka, T., Takahashi, K., Tsubaki, K., Hirata, M., Yamamoto, K., Biswas, A.,
Moriyama, T., Kawamura, Y., 2018. Isolation and characterization of acid-soluble
bluefin tuna (Thunnus orientalis) skin collagen. Fish Aquatic Sci 21, 1–8.
Tassara, E., Orel, B., Ilan, M., Cavallo, D., Dodero, A., Castellano, M., Vicini, S.,
Giovine, M., Pozzolini, M., 2023. Seasonal molecular difference in fibrillar collagen
extracts derived from the marine sponge Chondrosia reniformis (Nardo, 1847) and
their impact on its derived biomaterials. Mar. Drugs 21 (4), 210.
Tziveleka, L.A., Kikionis, S., Karkatzoulis, L., Bethanis, K., Roussis, V., Ioannou, E., 2022.
Valorization of fish waste: isolation and characterization of acid-and pepsin-soluble
collagen from the scales of mediterranean fish and fabrication of collagen-based
nanofibrous scaffolds. Mar. Drugs 20 (11), 664.
Vallejos, N., González, G., Troncoso, E., Zúñiga, R.N., 2014. Acid and enzyme-aided
collagen extraction from the byssus of Chilean mussels (Mytilus Chilensis): effect of
process parameters on extraction performance. Food Biophys. 9, 322–331.
Van Soest, R.W., Boury-Esnault, N., Vacelet, J., Dohrmann, M., Erpenbeck, D., De
Voogd, N.J., Santodomingo, N., Vanhoorne, B., Kelly, M., Hooper, J.N., 2012. Global
diversity of sponges (Porifera). PLoS ONE 7 (4), e35105.
Vate, N.K., Strachowski, P., Undeland, I., Abdollahi, M., 2023. Structural and functional
properties of collagen isolated from lumpfish and starfish using isoelectric
precipitation vs salting out. Food Chem.: X 18, 100646.
Veeruraj, A., Arumugam, M., Ajithkumar, T., Balasubramanian, T., 2015. Isolation and
characterization of collagen from the outer skin of squid (Doryteuthis singhalensis).
Food Hydrocoll. 43, 708–716.
Venmathi Maran, B.A., Jackson, A., Ananthan, T., Kumar, M., 2023. Biotechnological
applications of jellyfish-derived products. Marine Biotechnology: Applications in
Food, Drugs and Energy. Springer Nature Singapore, Singapore, pp. 245–270.
Wang, L.S., Shi, Z., Shi, B.M., Shan, A.S., 2014. Effects of dietary stevioside/rebaudioside
A on the growth performance and diarrhea incidence of weaned piglets. Anim. Feed
Sci. Technol 187, 104–109.
V. Prajaputra et al.
Wang, L., Wang, X., Bai, F., Fang, Y., Wang, J., Gao, R., 2019. The anti-skin-aging effect
of oral administration of gelatin from the swim bladder of Amur sturgeon (Acipenser
schrenckii). Food Funct 10 (7), 3890–3897.
Wang, Z., Zeng, Q., Zhang, X., 2015. Isolation and purification of antitumor and anti-
aging peptides from spirulina platensis. Amino Acids 47 (8), 1649–1650.
SACHSENPLATZ 4-6, PO BOX 89, A-1201 WIEN, AUSTRIA: SPRINGER WIEN.
Widdowson, J.P., Picton, A.J., Vince, V., Wright, C.J., Mearns-Spragg, A., 2018. In vivo
comparison of jellyfish and bovine collagen sponges as prototype medical devices.
J. Biomed. Mater. Res. Part B. 106 (4), 1524–1533.
Wilkie, I.C., Candia Carnevali, M.D., 2023. Morphological and physiological aspects of
mutable collagenous tissue at the autotomy plane of the starfish Asterias rubens L.
(Echinodermata, Asteroidea): an echinoderm paradigm. Mar. Drugs 21 (3), 138.
Yan, N., Chen, X., 2015. Sustainability: don’t waste seafood waste. Nature 524 (7564),
155–157.
Yemisken, E., Jiménez-Rosado, M., Perez-Puyana, V., Sancar, S., Bektaş, S., Yildiz, T.,
Eryilmaz, L., Romero, A., 2023. Alternative sources of marine bioactive compounds
211
South African Journal of Chemical Engineering 47 (2024) 197–211
from the black sea: isolation and characterization of fish skin collagen from
Neogobius melanostomus (Pallas 1814) (Perciformes: gobiidae). Reg. Stud. Mar. Sci.
60, 102887.
Zehlila, A., Schaumann, A., Mlouka, A.B., Bourguiba, I., Hardouin, J., Masmoudi, O.,
Cosette, P., Amri, M., Jouenne, T., 2017. Glioprotective effect of Ulva rigida extract
against UVB cellular damages. Algal Res. 23, 203–215.
Zhang, J., Duan, R., Huang, L., Song, Y., Regenstein, J.M., 2014. Characterisation of acid-
soluble and pepsin-solubilised collagen from jellyfish (Cyanea nozakii Kishinouye).
Food Chem. 150, 22–26.
Zhuang, Y.L., Sun, L.P., 2012. Anti-melanogenic activities of collagen peptides from
jellyfish (Stomolophus meleagris). In: Advanced Materials Research, 343. Trans Tech
Publications Ltd, pp. 505–512.
Zu, X.Y., Li, M.J., Xiong, G.Q., Cai, J., Liao, T., Li, H.L., 2023. Silver carp
(Hypophthalmichthys molitrix) scales collagen peptides (SCPs): preparation,
whitening activity screening and characterization. Foods 12 (7), 1552.