Research Article

Received: 18 June 2018 Revised: 20 September 2018 Accepted article published: 23 October 2018 Published online in Wiley Online Library: 24 January 2019

(wileyonlinelibrary.com) DOI 10.1002/jsfa.9438

A comparison of physicochemical
characteristics, texture, and structure
of meat analogue and meats
Sasimaporn Samard and Gi-Hyung Ryu*

Abstract
BACKGROUND: The continuous increase of global consumer’s dietary behaviors towards reducing meat consumption due to
health benefits, ecological, ethical, and social aspects. Texturized vegetable protein (TVP) transformed from plant protein-based
ingredient can impart fibrous structure like muscle meat. However, there is limited information on a comparison of product
properties of TVP and meats. In this study, the comparison of physicochemical properties, texture, and structure of TVP and
different types of meats (beef, pork, and chicken) were investigated.

RESULTS: The nitrogen solubility and integrity index, chewiness and cutting strength of TVP were similar to that of the chicken
sample compared to other meats. However, water absorption capacity of TVP (2173.84 g kg−1 ) was significantly higher than
all meat samples (1095.37 to 1653.52 g kg−1 ). The color and amino acids of TVP were different from meat samples due to the
difference in protein types. TVP showed a fibrous structure with non-uniform air cells.

CONCLUSION: The study demonstrated that some textural and chemical characteristics of texturized vegetable protein under
intermediate moisture extrusion exhibited the most similarity to chicken meat.
© 2018 Society of Chemical Industry

Keywords: texturized vegetable protein; meat analogue; plant protein; texture; structure; meat

INTRODUCTION buying motives of consumers.5 Several researchers revealed that

The reduction in consumption of meat in the dietary behaviors
of global consumers has been increasing due to the concerns
about the wellbeing from health, ecological, ethical, and social
aspects.1 The consumption of plant protein-based diet tends to
lower in body weight, cholesterol, and blood pressure levels, which
leads to the reduction in the risk of stroke, heart disease, and
cancers.2 Therefore, the replacement of meat protein with plant
protein in the human diet has been receiving attention from
both academic and industrial researches.1,3–5 Nevertheless, the
introduction of new forms of food products that utilize plant
protein is critical.6
Meat analogue or texturized vegetable protein (TVP) is a
plant-based protein product that contains highly beneficial
essential amino acid compositions, low saturated fat, and
cholesterol-free.7–9 Currently, TVP products can be divided
by mimicking ground, comminuted, and whole muscle meat
products.4 Within these three TVP products, our study emphasizes
on the last category of TVP, which contains intermediate moisture
content and indicates the fibrous structure that resembles meat
muscle. The low/intermediate moisture TVP has avaiability at
ease of handling, storage, and shelf stability, which requires time
to hydrate prior to consumption. Upon hydration, its structure
presents a fibrous structure mimicking that of meat.7,9 Moreover,
TVP has a competitive edge in the market against animal meat as
it is cheaper than meat.3,6
Earlier work reported that the similarity of TVP and meat, in terms
2708
the utilizing of soy protein and wheat gluten as TVP ingredients
could impart texture, appearance, taste, smell, functionality, and
nutrition similar to that of meat.3,8,10,11 Although, many researchers
explored that TVP from these ingredients could texturize as similar
to meat muscle, the study of a comparison of characteristics of TVP
and meats has not been done before. Furthermore, soy protein
and wheat gluten are availability at a reasonable cost.3,11 Recently,
the effect of wheat gluten and moisture contents on texturization
of extruded soy protein has been examined by Park et al.12 They
reported that TVP with 600 g kg−1 wheat gluten content and
450 g kg−1 moisture content could form the fibrous structure. Thus,
the blend of soy protein and wheat gluten in the ratio of 40:60
under (450 g kg−1 ) intermediate moisture extrusion is selected for
this research.
Beef, pork, and chicken meats are chosen for comparing the
characteristics with TVP in this study because these meats are
three most consumed meat in 2017 globally,13 which have a
different composition of water, proteins, fats, vitamins, minerals,
carbohydrates, and other bioactive components. Beef and pork
∗ Correspondence to: GH Ryu, Department of Food Science and Technology, Food
and Feed Extrusion Research Center, Kongju National University, Daehakro 54,
Yesan, Chungnam 32439, Republic of Korea. E-mail: ghryu@kongju.ac.kr
Department of Food Science and Technology, Food and Feed Extrusion
Research Center, Kongju National University, Daehakro 54, Yesan, Chungnam,

of appearance and eating sensation, essentially influenced the Republic of Korea

J Sci Food Agric 2019; 99: 2708–2715 www.soci.org © 2018 Society of Chemical Industry
A comparison of physicochemical characteristics, texture, and structure of meat analogue and meats
Figure 1. Schematic diagram of screw configuration of co-rotating intermeshing twin screw-extruder (model THK 3).
meats are classified as red meat which contains a large amount
of myoglobin, while a chicken meat is classified as white meat
under poultry which contains the low amount of myoglobin.14
First, the purpose of the present study was to investigate the
physicochemical characteristics, texture, and microstructure of
intermediate moisture TVP. Second, it was done to compare the
product characteristics of TVP with three meats including beef,
pork, and chicken meats.
MATERIALS AND METHODS
Materials
Isolated soy protein (ISP) and vital wheat gluten (WG) were
obtained from Wachsen Industry Co. (Quingdao, China)
and Roquette Freres (Lestrem, France), respectively. The pro-
tein content of ISP and WG were indicated 900 and 830 g kg−1
(dry basis), respectively. The moisture content of 62 g kg−1 was
observed in both ISP and WG. Fresh lean meats were purchased
from regional supermarkets in Chungnam, Korea: beef round
steak, pork loin, and skinless chicken breast.
Extrusion process
TVP from the mixture of ISP and WG in the ratio of 40:60 (w/w) was
texturized with a co-rotating intermeshing twin-screw extruder
by Incheon Machinery Co., Ltd., Korea (Fig. 1). The experiment
was carried out using a screw configuration with screw length
to diameter (L/D) ratio of 23:1, 69 cm barrel length, 3 cm screw
diameter (Fig. 1), and equipped with a slit die of 1 cm width,
0.45 cm height, and 4.97 cm length (Fig. 2). Extrusion parameters
were as follows: 0.1 kg min−1 feed rate, 450 g kg−1 feed moisture,
250 rpm screw speed and 140 ∘ C die temperature as proposed by
Park et al.12 After extrusion, the sample was dried directly in an
Figure 2. Die configuration of twin screw-extruder.
J Sci Food Agric 2019; 99: 2708–2715 © 2018 Society of Chemical Industry
www.soci.org
oven (OF-22GW, Jeio Tech Co., Ltd., Gyeonggi, Korea) at 50 ∘ C for
12 h and the dried pellet was stored in zip-lock plastic bags at room
temperature to analyze its textural properties. The dried pellets
were finely pulverized to a particle size of 30 mesh (US Standard
Sieve Series) by a stainless-steel mixer (FM-909 T, Hanil Electrical
Co., Seoul, Korea). The powder was maintained in zip-lock plastic
bags at room temperature until further use.
Preparation of freeze-dried meat samples
Samples of beef, pork, and chicken were washed and cut into
cubes (approximately 1.5 × 1.5 × 1.5 cm3 ). The cubed meats were
treated under two different conditions: raw and cooked meat
samples. For cooked meat sample, the cubed meat was boiled at
100 ∘ C for 10 min as proposed by Choi et al.15 Both raw and cooked
meats were drained for 15 min by using 20 mesh. Samples were
frozen at -70 ∘ C for 24 h in a freezer (Model CLN-32 U, Ilwon Freezer
Co., Ltd., Gyeonggi, Korea). Frozen samples were placed and dried
in a freeze-dryer (Model TFD5505, Ilshin Lab Co., Ltd., Gyeonggi,
Korea) at a pressure of 0.67 Pa and the condensation temperature
of −60 ± 2 ∘ C for 48 h. The freeze-dried meat samples were kept
in zip-lock plastic bags at room temperature until the analysis
of texture and microstructure. The samples were ground to fine
powder, passed through 30 mesh and were stored in zip-lock
plastic bags at room temperature until measurements.
Physicochemical property
Color
The color of ground samples was measured with a colorimeter
(Minolta CR-300, Osaka, Japan) as lightness (L), redness (a), and
yellowness (b). The colorimeter was calibrated against a standard
white tile (L = 92.92, a = −0.32, and b = 3.72). Measurements
were conducted in triplicate. The L, a, and b values represent as
described by Santillán-Moreno et al.16 2709
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Nitrogen solubility index
Nitrogen solubility index (NSI) was measured by using slightly
modified methods.17 The ground sample (1.5 × 10−3 kg) was
extracted with 75 mL of 0.5% KOH and was agitated at 30 ∘ C,
1.29×g for 20 min using a shaker (SI-300R, Jeio Tech Co., Ltd.,
Seoul, Korea). The mixture was centrifuged at 804.96×g for 30 min
by the centrifuge (H-1000-3, Hanil Science Industrial Co., Gangne-
ung, Korea). The clear supernatant was collected and the soluble
nitrogen content then proceeded as described by Starcher,18 using
a ninhydrin assay. The total nitrogen content was also analyzed
according to the method of Starcher.18 Albumin was used as a
standard, and NSI was calculated as the following equations and
presented as an average of three readings.
( )
NSI g kg−1 = (Soluble nitrogen content
∕Total nitrogen content in sample) × 1000
Moisture and amino acid contents
Moisture content was determined by heating each sample to con-
stant weight at 105 ∘ C accordance with the standard methods
of AOAC.19 Determinations were conducted in triplicate. For amino
acid content, the sample hydrolysis was based on the standard
procedure of AOAC.20 Sulfur-containing amino acids (cysteine and
methionine) were first oxidized with performic acid and then
hydrolyzed with 6 N HCl at 110 ∘ C for 24 h under a nitrogen atmo-
sphere. After that, the hydrolysate samples were evaporated at
50 ∘ C, pH is adjusted to 2.2 with sodium citrate buffer, and indi-
vidual amino acid components are separated by Hitachi amino
acid analyzer (L-8800, Hitachi High-Technologies Co., Ltd., Seoul,
Korea) with ion exchange column (4.6 mm × 60 mm). The remain-
ing 15 amino acids (acid-stable amino acids) were proceeded by
the same step of sulfur-containing amino acids without the oxi-
dization. Quantitation was performed after ninhydrin derivatiza-
tion UV/Vis detection. Amino acids were detected at 570 nm; the
amino acid proline was also detected at 440 nm for better resolu-
tion. Amino acid concentrations were quantified against an exter-
nal amino acid standard (AA-S-18, Sigma Chemical Co., St. Louis,
Mo.) and were expressed in g kg−1 of protein. All samples were ana-
lyzed in duplicate.
Textural properties
Water absorption capacity
Water absorption capacity (WAC) was determined following
the method of Lin et al.21 The results were averaged from three
measurements.
Integrity index
Integrity index of the samples was slightly adapted from the proce-
dure of Park et al.12 The dried pellet sample (5 × 10−3 kg) was sus-
pended in 100 mL of distilled water and was soaked in a water bath
at 80 ∘ C for 30 min. Then, the soaked sample was pressurized and
heated immediately in an autoclave (PAC-60, Lab House Co., Ltd.,
Seoul, Korea) at 121 ∘ C for 15 min. The hydrated sample was trans-
ferred to the beaker with 100 mL distilled water and then was dis-
persed by IKA disperser (T10 Basic Ultra-Turrax, IKA Co., Ltd., Seoul,
Korea) at 17530xg for 1 min. After that, it was passed through the
sieve of 20 mesh and was dried at 105 ∘ C until equilibrium. Mea-
surements were performed in triplicate for each sample. Integrity
index was calculated by using the following equation.
( )
2710
Integrity index g kg−1 = (Dry residue wt.∕Sample wt.) × 1000
wileyonlinelibrary.com/jsfa © 2018 Society of Chemical Industry
S Samard, G-H Ryu
Texture profile analysis and cutting strength
Texture profile analysis (TPA) of the sample was conducted
with a Sun rheometer (Compac-100, Sun Science Co., Japan)
by using a 25 mm-diameter cylinder probe. The dried TVP pellet
and freeze-dried cooked meat samples were hydrated at 80 ∘ C
for 30 min, while the fresh meat was cooked at 100 ∘ C for 10 min.
Then, the samples were drained for 15 min using 20 mesh. The
texture analysis conditions were as follows: the cross-head speed
of 100 mm min−1 , the maximum peak stress of 10 kg and the
distance between two supports of 13 mm. The springiness,
cohesiveness, and chewiness were determined as described by
Breene.22 The cutting strength of both transversal and longitudi-
nal directions of samples was measured by using a cutting probe
(7.5 mm × 38.3 mm) equipped with a 2-kg maximum peak stress.
The results were averaged of ten treatments.
Microstructure
The microstructure was obtained by field emission scanning elec-
tron microscopy (MIRA III LMH, Tescan Co., Cranberry Township, PA)
with an accelerating voltage of 10 kV. The surface of samples was
sputter-coated with silver-palladium alloy and was fixed on the
studs. The micrograph of samples was taken in the longitudinal
direction at 500x magnification.
Statistical analysis
The experiments were analyzed by using IBM SPSS software ver-
sion 24.0 (IBM, Armonk, NY, USA). The mean comparison was done
by using Duncan’s multiple range tests. Differences on each treat-
ment were considered significant at P < 0.05.
RESULTS AND DISCUSSION
Physicochemical property
Color
The color parameters of TVP are significantly (P < 0.05) affected by
the extrusion process as shown in Table 1. The L value of TVP was
significantly lower than raw material, while the a and b values were
significantly higher. The color change during extrusion process
is influenced by Maillard reaction, caramelization, hydrolysis, as
well as, the degradation of pigments.16 The color parameters
of freeze-dried meats were significantly (P < 0.05) affected by
cooking and meat types (Table 1). The L values of pork and chicken
significantly increased after cooking but only L value of beef
sharply decreased (P < 0.05). The a values of all meats significantly
decreased after cooking (P < 0.05), compared to their raw meats.
In addition, the cooking led to an increase in the b values of
beef and pork but the reduction in chicken. The heating process
such as boiling influences the color change of meat products due
to the denaturation and oxidization of three forms myoglobin
(oxyMb, deoxyMb, and metMb) in meat, which produces different
colors.15,23 Moreover, the highest L value and the lowest a and b
values were observed in the chicken sample, compared to other
meats, which may be attributed to the meat type and myoglobin
content. Earlier work reported that the myoglobin content of
chicken was lower than pork and beef, respectively.14 The lower
myoglobin content led to reducing in redness and darkness of
meats. Furthermore, the color of TVP obviously showed different
from all cooked meats.
Nitrogen solubility index
NSI is a significant indicator which refers to the water-dispersible
nitrogen in the product and reflects the degree of cooking, protein
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Table 1. Physicochemical and textural properties of texturized vegetable protein and different types of freeze-dried meats

Color NSI WAC Integrity

Sample L a b (g kg−1 ) (g kg−1 ) index (g kg−1 )

Control Raw 81.34 ± 0.23c −1.32 ± 0.01h 17.18 ± 0.05b 451.80 ± 1.04a – –
TVP 70.00 ± 0.11f 0.99 ± 0.02f 25.56 ± 0.03a 359.14 ± 0.64d 2173.84 ± 49.84a 733.68 ± 1.85f
Beef Raw 50.08 ± 0.02g 11.39 ± 0.03a 13.41 ± 0.02d 286.04 ± 3.74g 1261.03 ± 5.23e 906.95 ± 4.04a
Cooking 45.07 ± 0.17h 7.44 ± 0.02b 14.12 ± 0.07c 247.03 ± 0.24h 1095.37 ± 61.44f 911.13 ± 6.44a
Pork Raw 71.30 ± 0.13e 5.05 ± 0.01c 12.40 ± 0.03e 370.72 ± 2.13c 1432.35 ± 39.94cd 843.62 ± 4.04c
Cooking 72.57 ± 0.18d 3.18 ± 0.05d 13.76 ± 0.09cd 314.03 ± 0.74f 1317.38 ± 20.71de 867.91 ± 1.12b
Chicken Raw 82.16 ± 0.15b 1.90 ± 0.01e 12.05 ± 0.07e 434.02 ± 3.43b 1653.52 ± 48.05b 791.99 ± 0.31e
Cooking 83.94 ± 0.03a −0.21 ± 0.05g 11.56 ± 0.03f 344.22 ± 1.33e 1492.91 ± 92.03c 806.45 ± 4.62d

Different letters (a-h) in the same column are significantly different at P < 0.05.
Values are means of triplicate ± standard deviation.

denaturation, and protein digestibility.17 The difference of solubil-
ity between the native and thermally denatured texturized protein
is used to analyze the degree of texturization that occurs during
the manufacture of meat analogue.24 NSI of TVP (359.14 g kg−1 )
is significantly lower than that of raw material (451.80 g kg−1 ) as
shown in Table 1. This might be the effect of protein denaturation
during extrusion, which resulted in higher protein digestibility,
lower protein solubility, and led to increasing in insoluble protein
or protein texturization.7,9,25 A similar result was observed in the
freeze-dried meat samples. The NSI of meat samples significantly
decreased after cooking (P < 0.05), the highest decrease in NSI was
shown in the chicken sample, followed by pork, and the lowest
beef. Warner et al.26 explained that the sample which indicated a
high extent of protein denaturation dependent on myofibrillar and
sarcoplasmic proteins. In addition, compared to all of the meats,
the NSI of TVP (359.14 g kg−1 ) was similar to the NSI of cooked
chicken (344.22 g kg−1 ) and the ratio of decrease in NSI after heat-
ing for both TVP (20.52%) and chicken (20.69%) were also similar.
Moisture and amino acid contents
The effects of heat treatments on the moisture and amino acid con-
tents of TVP and different freeze-dried raw and cooked meats are
shown in Table 2. The moisture content of TVP was significantly
(P < 0.05) higher than that of raw material which resulted in reduc-
tion in total amino acid contents. On the other hand, the mois-
ture contents of meat samples were significantly (P < 0.05) lower
than that of their raw meats which led to increasing in total amino
acid contents due to the water loss. The major amino acids of
plant protein both raw and TVP were glutamic acid, aspartic acid,
proline, and leucine which were similar to that of extruded soy-
bean/corn flour.27 Meanwhile, glutamic acid, aspartic acid, lysine,
and leucine were identified as the major amino acids in meat sam-
ples, which were in agreement with the results for beef,28 pork29 ,
and chicken30 , where glutamic acid, aspartic acid, and leucine were
the amino acids present at a higher level. The sulfur-containing
amino acids (methionine, cysteine), glutamic acid and proline of
TVP were higher than that of raw material but the other amino
acids were lower. Guzmán-Ortiz et al.27 described that the increase
of sulfur amino acids in extruded soybean/corn flour was due
to the protein texturization during extrusion cooking, whereas
lysine, arginine, and phenylalanine decreased. Among essential
amino acids presented losses after extrusion, lysine was the most
unstable amino acid in this study, which was in accordance with
the finding of Dias-Paes and Mega31 with losses in the range of
Maillard reaction and the formation of bonds between lysine and
glucose,33 which may be led to higher a and b values of TVP in
this study. Dias-Paes and Mega31 found the negative correlation
between lysine content and color parameters.
The amino acids of plant protein (TVP) obviously showed differ-
ent from all cooked meats. Comparison of essential amino acids
between TVP and cooked meats revealed that all essential amino
acids of TVP were lower than cooked meats but only phenylalanine
exhibited higher. For non-essential amino acids, alanine, arginine,
aspartic acid, and glycine of TVP were lower than cooked meats,
while cysteine, proline, serine, and particularly glutamic acids were
higher than cooked meats.
Textural properties
Water absorption capacity
WAC is an essential parameter that indicates the quality of the
product, which relates to texture after hydration.21,34,35 Table 1
shows the WAC ranging from 1095.37 to 2173.84 g kg−1 . The
WAC of TVP (2173.84 g kg−1 ) was significantly (P < 0.05) higher
than those of freeze-dried meats (1095.37–1653.52 g kg−1 ),
which may be attributed to protein types, protein-water
interactions, water–water interactions, conformational char-
acteristics, as well as, structures.21,35 The porosity of extrudate
directly affected the WAC.35 The highest WAC in meat samples
was found in chicken samples (1492.91–1653.52 g kg−1 ), fol-
lowed by pork (1317.38–1432.35 g kg−1 ), and the lowest beef
(1095.37–1261.03 g kg−1 ). Köhn et al.34 described that myofibrillar
proteins (actin and myosin), intramuscular connective tissue, and
perimysium of meat played the major roles in WAC. Besides, the
WAC values of cooked meat samples were lower than that of their
raw meats. It might be interpreted that the structure of cooked
meat was destroyed by heating, which led to the shrinkage of
meat fiber and connective tissue, consequently, this structure held
less water retention.
Integrity index
Integrity index is an important texture parameter which affects
the yield and quality of TVP. Integrity index refers to the texture
residues of meat analogue after the pellet sample is hydrated, pres-
surized, dispersed, and dried.12,36 Integrity index values of TVP and
different freeze-dried meats range from 733.68 to 911.13 g kg−1
as presented in Table 1. The integrity index of TVP (733.68 g kg−1 )
was lower than that of the integrity index of freeze-dried meats
(806.45–911.13 g kg−1 ). The integrity index values of beef sam-
2711

12–49%.27,32 The main cause of reduction of lysine is due to the ples (906.95–911.13 g kg−1 ) were significantly higher than that of

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Table 2. Moisture and amino acid contents of texturized vegetable protein and different types of freeze-dried meats

Control Beef Pork Chicken

Raw TVP Raw Cooking Raw Cooking Raw Cooking

Moisture content (g kg−1 ) 51.23 ± 1.25e 68.20 ± 1.55ab 66.50 ± 1.00b 60.40 ± 1.11c 69.63 ± 0.57a 54.83 ± 2.47d 59.10 ± 2.18c 56.17 ± 2.00d
Amino acids (g kg−1 protein)
Essential amino acids
Histidine 19.50 ± 1.15 18.41 ± 0.13 27.60 ± 1.23 23.72 ± 0.13 33.91 ± 0.16 30.21 ± 0.14 29.60 ± 0.34 28.51 ± 0.12
Isoleucine 34.52 ± 0.54 32.32 ± 0.14 31.42 ± 0.43 37.13 ± 1.12 38.65 ± 2.13 41.52 ± 0.15 40.81 ± 1.25 44.21 ± 1.25
Leucine 61.32 ± 2.12 55.28 ± 1.24 55.71 ± 0.12 60.40 ± 0.13 67.00 ± 3.42 73.10 ± 0.78 68.67 ± 4.52 74.80 ± 3.25
Lysine 36.20 ± 0.28 28.58 ± 0.16 58.00 ± 0.11 68.76 ± 0.24 72.28 ± 2.36 77.28 ± 2.45 75.73 ± 2.31 80.70 ± 1.08
Methionine 12.01 ± 0.15 12.24 ± 0.02 18.01 ± 0.15 22.01 ± 0.34 23.87 ± 0.45 25.26 ± 0.37 24.21 ± 0.17 26.00 ± 0.35
Phenylalanine 42.81 ± 3.24 41.80 ± 1.54 28.59 ± 0.56 30.04 ± 0.86 33.75 ± 1.89 37.00 ± 0.96 34.47 ± 0.65 37.51 ± 0.34
Threonine 27.72 ± 1.25 25.77 ± 1.24 31.27 ± 1.40 36.86 ± 0.91 38.49 ± 1.23 41.90 ± 1.56 39.03 ± 0.24 41.82 ± 0.12
Valine 37.71 ± 1.87 35.48 ± 0.86 34.85 ± 1.50 40.21 ± 1.43 42.10 ± 2.34 45.83 ± 1.23 44.01 ± 1.70 47.12 ± 2.35
Non-essential amino acids
Alanine 29.60 ± 2.18 26.80 ± 0.15 39.62 ± 1.67 40.32 ± 0.45 46.00 ± 1.24 51.43 ± 1.25 48.90 ± 3.51 52.31 ± 1.25
Arginine 49.46 ± 3.08 42.47 ± 1.26 41.81 ± 2.13 50.04 ± 0.12 51.77 ± 1.30 58.43 ± 0.25 55.12 ± 4.61 58.61 ± 0.57
Aspartic acid 68.02 ± 2.16 58.90 ± 1.28 63.28 ± 1.45 64.18 ± 2.13 76.90 ± 0.85 84.70 ± 3.76 80.50 ± 2.42 86.63 ± 2.60
Cystine 12.81 ± 0.12 13.80 ± 0.45 7.30 ± 0.21 9.02 ± 0.05 9.61 ± 0.23 10.04 ± 0.45 9.10 ± 0.04 10.00 ± 0.06
Glycine 31.28 ± 1.26 29.56 ± 2.18 29.52 ± 0.34 34.18 ± 0.12 33.25 ± 0.34 42.64 ± 1.23 35.71 ± 1.24 37.01 ± 2.18
Glutamic acid 210.18 ± 4.65 229.59 ± 5.46 101.42 ± 2.11 108.31 ± 6.21 123.25 ± 4.45 133.14 ± 5.23 124.00 ± 7.35 133.12 ± 5.27
Proline 64.00 ± 1.23 70.40 ± 4.27 25.17 ± 0.67 30.28 ± 1.27 29.90 ± 1.25 36.08 ± 2.12 28.90 ± 1.28 31.32 ± 1.25
Serine 41.15 ± 1.10 40.41 ± 2.34 26.87 ± 0.12 31.29 ± 1.20 32.47 ± 0.56 36.12 ± 1.34 33.81 ± 1.06 36.01 ± 1.10
Tyrosine 30.26 ± 1.05 28.52 ± 1.24 28.50 ± 0.23 29.20 ± 0.34 25.90 ± 1.25 20.40 ± 1.50 23.80 ± 1.00 24.90 ± 1.24
Total amino acids 808.55 790.33 648.94 715.95 779.10 845.08 796.37 850.58

Different letters (a-e) in the same row are significantly different at P < 0.05.
Moisture content values are means of triplicate ± standard deviation.
Amino acids values are means of duplicate ± standard deviation.

pork (843.62–867.91 g kg−1 ) and chicken (791.99–806.45 g kg−1 ),
respectively (P < 0.05). Beef sample performed the strongest tex-
ture which was hard to destroy by high pressure and temperature
during autoclaving and homogenization. The integrity index of
TVP (733.68 g kg−1 ) in the present study is similar to the integrity
index of texturized ISP-WG mixture 71.15% (711.5 g kg−1 ) from the
finding of Park et al.12 Compared to all of the meats, the integrity
index of TVP had the most similarity to that of chicken samples.
Moreover, the negative correlation and the R2 of 0.831 are
established in the correlation between the average of integrity
index and NSI of TVP and different types of cooked meats as
shown in Fig. 3(A). Integrity index of samples increased when
the solubility of samples decreased. Our finding was consistent
with the research conducted by Gu and Ryu36 who presented the
integrity index of extruded ISP at different conditions increased
when solubility decreased.
Texture profile analysis and cutting strength
TPA and cutting strength in transversal and longitudinal direc-
tions of TVP, cooked meats, and freeze-dried cooked meats are
presented in Table 3. The springiness, cohesiveness, chewi-
ness, transversal, and longitudinal cutting strength of TVP
were indicated 87.92%, 75.02%, 2.96 kg, 12 397.60 kg m−2 , and
8022.21 kg m−2 , respectively, which were significantly different
from meat samples (P < 0.05). Comparison of three meats showed
that the highest cutting strength in transversal and longitudinal
was indicated in beef samples, while the lowest was obtained in
chicken samples. The different types of meats showed different
TPA and cutting strength which may be related to the difference
in proportion, distribution, and natural composition of muscle
2712
collagen, elastin, and fat density.37 Besides, the transversal cutting
strength of TVP and all meat samples was slightly higher than that
of their longitudinal cutting strength, which also reported for the
texture of extruded ISP.36 It is stated that the cutting strength in
vertical and parallel directions of extrudates could indicate the
texturization degree or fibrous structure formation.38 Moreover,
it can be seen from Table 3 that there was no significant differ-
ence in chewiness of TVP (2.96 kg), cooked beef (2.94 kg), cooked
pork (3.17 kg), cooked chicken (2.84 kg), and freeze-dried cooked
chicken (2.74 kg). Although the cutting strength of TVP was sig-
nificantly different from all meat samples, the cutting strength of
TVP was closest to the freeze-died cooked chicken.
The relation between types of samples, the average of transver-
sal and longitudinal cutting strength of TVP and different types of
freeze-dried cooked meats are presented in Fig. 3(B). The negative
relations were observed in both transversal and longitudinal cut-
ting strength when the samples were arranged from freeze-dried
cooked beef, pork, chicken, and TVP, respectively, while, the pos-
itive correlation and the R2 of 0.9631 were indicated in the corre-
lation between the average of longitudinal cutting strength and
integrity index of samples (Fig. 3(C)).
Microstructure
Texturization is the process of converting protein aggregate to a
fibrous structure. Extruders could restructure vegetable-based
proteins to form fibrous structures similar to textures of meat
tissues.7,9,39 The scanning electron microscopy (SEM) was used to
view the longitudinal microstructures of TVP (A) and different raw
and cooked meats as displayed in Fig. 4. TVP from this study could

such as the myofibrillar proteins, the connective tissue proteins, completely texturize because of high protein concentration and

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(A) (B) Cutting strength (kg m-2)

400
Nitrogen soubility index (g kg-1)

Beef
24000 24000

360 Pork
20000 20000
Chicken

320 TVP
16000 16000

280 12000 12000

y = -0.5876x + 803.72
R2 = 0.831
240 8000 Transversal direction
8000
Longitudinal direction
200 4000 4000
700 750 800 850 900 950 Beef Pork Chicken TVP
Integrity index (g kg-1)

(C)16000
Cutting strength (kg m-2)

14000
y = 41.563x - 22859
12000 R2 = 0.9631

Beef
10000
Pork

8000 Chicken

TVP
6000
700 750 800 850 900 950
Integrity index (g kg-1)

Figure 3. Correlations between nitrogen solubility and integrity index (A), transversal and longitudinal cutting strength (B), and longitudinal cutting
strength and integrity index (C) of texturized vegetable protein and different types of freeze-dried cooked meats.

Table 3. Texture properties of texturized vegetable protein and different types of cooked and freeze-dried cooked meats

Cutting strength (kg m−2 )

Springiness Cohesiveness Chewiness
Sample (%) (%) (kg) Transversal direction Longitudinal direction

TVP 87.92 ± 3.49a 75.02 ± 1.93b 2.96 ± 0.37b 12 397.60 ± 694.51e 8022.21 ± 822.62e
Beef -a 69.12 ± 8.48b 64.79 ± 9.68c 2.94 ± 0.40b 19 010.50 ± 1198.72a 17 928.30 ± 1860.63a
FDb 71.21 ± 7.47b 66.13 ± 5.87c 5.13 ± 0.59a 19 575.91 ± 1138.13a 14 973.72 ± 1267.41b
Pork - 71.44 ± 2.87b 59.20 ± 3.01d 3.17 ± 0.43b 16 220.77 ± 1140.51c 15 345.14 ± 713.101b
FD 62.57 ± 1.68a 86.24 ± 2.26a 5.00 ± 0.53a 17 374.82 ± 747.51b 13 734.33 ± 1431.82c
Chicken - 58.00 ± 5.67c 49.35 ± 3.40e 2.84 ± 0.45b 14 751.84 ± 743.80d 10 320.32 ± 900.51d
FD 57.67 ± 6.28c 55.42 ± 5.59d 2.74 ± 0.30b 14 725.02 ± 893.11d 9787.53 ± 908.63d
a-: cooked meat.
bFD: freeze-dried cooked meat.
Different letters (a-e) in the same column are significantly different at P < 0.05.
Values are means of ten replicate ± standard deviation.

high protein abilities to impart texture. The cell structure of TVP shrinkage of the connective tissue.40,41 Comparison of TVP and
illustrated directional and fibrous structure with non-uniform air meat microstructures revealed that TVP formed the directional
cells which was influenced by low extrusion moisture (450 g kg−1 ) and fibrous arrangement like meat structure but different in
equipped with the slit die. The texturization occurs during extru- amount and shape of air cells, consequently, leading to differences
sion due to protein structures are unfolded, realigned, hydrolyzed, in water absorption, springiness, and cohesiveness.
and denatured, consequently, protein solubility decreases and
cross-linking occurs.7,39
The changes in the structure of beef, pork, and chicken after CONCLUSION
cooking are demonstrated in Fig. 4; B1-B2, C1-C2, and D1-D2, The results obtained from this study presented that TVP from
respectively. The microstructure of all cooked meats (B2, C2 and 400 g kg−1 ISP and 600 g kg−1 WG extruded at 450 g kg−1 mois-
D2) became denser and more compact in fiber arrangements, ture extrusion cooking could be texturized and provided some
compared to that of their raw structures (B1, C1 and D1), which chemical and textural properties (NSI, integrity index, chewiness,
may be attributed to the combination of water loss, destruc- and cutting strength) similar to that of chicken meat, compared
tion of cell membrane, transversal shrinkage of meat fibers, the to pork and beef samples. The directional and fibrous structure
2713

aggregation and gel formation of sarcoplasmic proteins, and the with great air cells were observed in TVP which led to different

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 www.soci.org
Figure 4. Scanning electron micrographs of texturized vegetable protein (A) and raw and cooked beef (B1-B2), pork (C1-C2) and chicken (D1-D2).
from meat samples in WAC, springiness, and cohesiveness. Color
and amino acids of TVP presented difference from all of the meat
samples. Although the physicochemical characteristics, texture,
and microstructure of this TVP did not obviously show similar to
meats, this sample provided the valuable basic data for the devel-
opment of TVP further. Therefore, in order to successfully texturize
the highly fibrous meat analogue that is closest to the real chicken
muscle, further investigations of a combination of plant protein
ingredients, reducing sugar, and meaty flavor by using extrusion
condition are necessary.
ACKNOWLEDGEMENT
This work was supported by the research grant of the Kongju
National University in 2018.
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