Grupo 2 Ghanghas 2020 FRI Rice

Food Reviews International
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Classification, Composition, Extraction, Functional

Modification and Application of Rice (Oryza sativa)
Seed Protein: A Comprehensive Review
Neeraj Ghanghas, Mukilan M. T., Shikha Sharma & Pramod K. Prabhakar
To cite this article: Neeraj Ghanghas, Mukilan M. T., Shikha Sharma & Pramod K. Prabhakar
(2020): Classification, Composition, Extraction, Functional Modification and Application of Rice
(Oryza�sativa) Seed Protein: A Comprehensive Review, Food Reviews International, DOI:
10.1080/87559129.2020.1733596
To link to this article: https://doi.org/10.1080/87559129.2020.1733596
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FOOD REVIEWS INTERNATIONAL
https://doi.org/10.1080/87559129.2020.1733596
Classification, Composition, Extraction, Functional

Modification and Application of Rice (Oryza sativa) Seed
Protein: A Comprehensive Review
Neeraj Ghanghas , Mukilan M. T., Shikha Sharma, and Pramod K. Prabhakar
Department of Food Science and Technology, National Institute of Food Technology Entrepreneurship and
Management, Kundli, India
KEYWORDS
ABSTRACT food and allied industry;
functional and therapeutic
Food industry is actively searching for sustainable, economical, and
properties; protein fraction;
high-quality protein source. Rice and its milling by-products prove to protein modification; rice
be cheap, high-quality sources of protein possessing immense nutri- seed protein
tional and functional benefits. Rice seed protein (RSP) content and its
quality, amino acid profile and fractions (i.e. albumin, globulins,
prolamins and glutelins) have significant varietal influence. The func-
tional properties (solubility, foaming properties, oil and water absorp-
tion, emulsification properties, etc.) depend on various factors such as
extraction method, treatments, pH, concentration of salt & sugar in
the foods. RSP has low solubility but various protein modification
treatments have resulted in significant improvement in its solubility
and other consumer preferential properties. RSP exhibits some ther-
apeutic and nutraceutical properties such as hypoallergenic, antitu-
mor, anti-atherosclerotic, antigenic properties with sound amino acid
profile and substantial biological value. It can be used for biopolymer,
bioactive compound delivery system, and effective natural antioxi-
dant, treatment of hypertension and also for baby food formulations.
This review discusses grain structure, composition, protein types,
protein quality, extraction methods, functional properties and its
modification. RSP is exceedingly comparable to existing protein
sources such as soy, casein and fenugreek. Thus, RSP may be con-
sidered as a potential ingredient for food and allied industry.
CONTACT Pramod K. Prabhakar pramodkp@niftem.ac.in Department of Food Science and Technology, National
Institute of Food Technology Entrepreneurship and Management, Kundli, India
© 2020 Taylor & Francis
2 N. GHANGHAS ET AL.
Introduction
Rice (Oryza sativa) is one of the most important cereal crops cultivated across more than 100
countries across the globe. Rice is considered as the staple food, it feeds more than half of the
world population. India is the second-largest producer of rice in the world after china with an
output of 165.02-million-ton paddy in the year 2017 and also is the second largest in term of
total consumption of milled rice with consumption of 97.35 million ton.[1] It is mainly
consumed in boiled/cooked form. The two major sub-classes of Oryza sativa are japonica
which is sticky and short grain while Indica is non-sticky and long grain. Japonica is cultivated
in the areas of South-East Asian upland, temperate East Asia and South Asian high elevations,
while Indica is cultivated mainly in low-land areas of tropical Asia.[2]
Rice is nutritious and shows some unique functional properties which include hypo-
allergenicity and flavour-carrying capability.[3] White rice is most widely consumed while
there are also other cultivars such as red rice, black rice and brown rice which contain colour
pigments. The name of these varieties is due to the colour of their kernel (red, purple or black),
the deposition of the anthocyanins in various layers (aleurone, pericarp and seed coat) is
responsible for the different colour of the kernel.[4] According to Paine et al.,[5] golden rice is
the genetically modified rice variety which produces carotenoids in the endosperm, conferring
yellow colour to the grain. Suzuki et al.[6] reported that the black rice has higher protein,
vitamins and minerals which give it nutritional advantages over other common rice. Rice is
considered as the queen among the cereals due to its nutritional quality and higher
digestibility.[7] Rice seed protein is classified into four fractions, i.e. albumin, globulin, prola-
min and glutelin based on solubility in various solvents.[8] The seed storage proteins in rice
grain are present as protein bodies (PB-I & PB-II), these two protein bodies possess different
structure and composition.[9] Rice proteins have a sound amino acid profile comprising
essential amino acids such as threonine, leucine and phenylalanine along with sulphur-rich
amino acids like methionine and cysteine which are crucial for the human body. Rice proteins
contain high amount of methionine and phenylalanine as compared to casein. Amino acid
profile of foods is not only important in nutritional point of view but is also related to the
physical and chemical properties of the food product.[10–12] Rice and other sources of plant
proteins are abundantly available and are inexpensive with exceptional nutritive and func-
tional properties. The functional properties (solubility, foaming properties, oil and water
absorption, emulsification properties, etc.) of rice proteins are influenced by various para-
meters such as pH, salt & sugar concentrations; these parameters can be varied to modify and
exploit the functional properties of rice proteins for applications in different food
formulations.[13,14] Protein stability and functionality are crucial parameters that decide its
application in food and allied industries. The trend has shifted to protein modification in
recent years; researchers are exploring various conventional and novel treatments such as
micro-fluidization, high hydrostatic pressure treatment, enzymatic modification, chemical
modification, fermentation, ultrasonic treatment, microwave treatment, etc., for protein
modification. Protein modification helps to attain desired stability and functionality.
Rice has historically been a major part of an infant’s diet, it is generally among the first
solid foods introduced to a child post the weaning period and this is due to its superior
digestibility and hypoallergenic characteristics.[15] Rice proteins are also incorporated in
infant food supplements and baby foods due to their complete amino acid profile, they
have been shown to possess functional bioactive and anti-oxidative compounds that can
FOOD REVIEWS INTERNATIONAL 3
aid in treating cardiovascular ailments, gut functioning and allergies; thus acting as a novel
food ingredient.[16] They also show potential to act as filling and binding agents that
provide volume, texture, and mouth-feel to meat products such as sausages and salamis.
Protein films derived from rice have also been developed and tested for their mechanical
durability, vapour transmission, concentration effects and overall usage feasibility.[17]
Rice grain: structure and milling

Post-production activities of rice crop include harvesting, drying, storage and milling. Rice
is harvested in the form of rough rice after the maturation of the grain and is also known
as paddy. The harvesting time is of great economic significance because harvesting of the
unfilled and immature grains impacts the overall yield of the crop. Moisture content at the
time of harvesting is crucial as it affects the cost of drying, long-term safe storage, and
head rice yield at the time of milling.[18] Typically, the harvesting moisture content of rice
is above those required for long-term safe storage. The bulk moisture content as well as
the individual kernel moisture content distribution of the harvested rice influences the
milling quality. The general optimal harvest moisture content range to obtain maximum
head rice yield for long grain and medium grain rice cultivar is 19–22% and 22–24%,
respectively.[19,20]
The matured grain, i.e. paddy consists of tough siliceous hull inside which rice kernel is
enclosed. The rough rice seed comprises of the outermost layer, i.e. hull (16 – 28% dry mass
basis) and the caryopsis enclosed inside the hull.[21] The caryopsis contains white starchy
endosperm (89–94%), embryo (2–3%), pericarp (1–2%) and aleurone, seed coat & nucleus
together contributing 4–6% of the mass of caryopsis.[22] According to Verma et al.,[23,24] the
quality of rice is determined by various characteristics of the grain such as its appearance,
cooking quality, kernel dimensions, nutritional quality, and processing quality.
White rice and Brown rice are generally consumed in whole milled form and is
generally consumed after cooking. The methods of cooking involve pressure cooking,
steaming, or rapid boiling and the choice depends on the preference of the consumer and
the expected sensory quality of cooked rice. Rice milling process (Fig. 1) is a combination
of series of unit operations to transform the paddy into white-polished rice.[23,25] The
milling operation starts pre-cleaning unit operation, in this stage paddy is fed to the pre-
cleaner which removes foreign matter, chaff, straw, and empty grains. Pre-cleaned paddy
is passed through rubber rollers for de-husking of the grains; the aspirator is employed to
remove the husk from the mixture of brown rice and un-husked grains. The un-husked
grains are then removed using the separator and these un-husked grains are again
returned to the rubber rollers for de-husking while the brown rice is fed to the de-
stoner for removing stones and mud balls. The next stage of milling is the bran and
germ removal, which is also termed as whitening, the whitening operation is achieved by
using abrasive type and/or friction type milling system. The milled rice are fed to sifters to
remove small brokens, also known as brewer’s rice, while the rest of the rice grains are
transferred to the mist polisher to improve the appearance of the milled rice by removing
the leftover bran particles. A length grader, generally an indented cylinder is employed to
separate head rice and brokens and these are collected in separate bins. Based on the
requirement head rice and broken rice are blended in different ratios and bagged.[26]
Figure 1. Rice milling process; commercial rice milling systems. Source: [18].
Sotelo et al.[27] reported that polishing brown rice eliminates protein, ash, fat, and fibre
by 13%, 50%, 69%, and 66%, respectively, and these losses were calculated considering the
relative chemical composition and the percentage of each fraction (brown rice 100%, white
rice 91% and bran 9%) of rice grain.
Rice seed composition

Rice is a major source of nutrients for not only the population of India but also for the
people of several other countries where rice is consumed daily. Rice grains are a good
source of energy which is validated by various researches that have shown that it provides
348.79–370.53 kCal per 100 g.[4,7] Singh et al.[28] reported that the physical properties and
the composition get affected by the transplantation date of paddy.
The accumulation of lipid, protein and starch in the rice seed is affected by the cool
night time air temperature which in turn is a result of delayed transplantation. Sompong
et al.[4] studied the 13 coloured (Red & Black) rice varieties from different countries and
reported that the rice seed proximate composition in g/100 g DM basis, the 100 g rice
contains protein 7.16–10.85 g, moisture 9.28–13.12 g, ash 0.82–1.74 g, fat 1.15–3.72 g, total
dietary fibre 2.52–4.51 g and total carbohydrate 71.99–79.27 g. The proximate composi-
tion of different varieties is shown in Table 1.
Rice seed protein

The protein quality of rice seed has been found to be good among cereals due to its higher
digestibility (93%) exceptional biological value (74%) and PER (2.02–2.04%); however, it
contains a low amount of protein, i.e. 6–10%.[7] Various researchers have reported
Table 1. Proximate composition of rice (g/100 g DM basis).
Energy
Rice varieties Moisture Ash Fat Protein Total dietary fibre Total carbohydrate (kCal)
Red
Bahng Gawk 11.55 ± 0.04 1.33 ± 0.01 2.86 ± 0.02 9.21 ± 0.13 3.63 ± 1.30 75.04 ± 0.15 362.78 ± 0.24
Haek yah 12.38 ± 0.03 1.40 ± 0.01 2.91 ± 0.05 7.40 ± 0.11 4.18 ± 0.14 75.92 ± 0.11 359.43 ± 0.30
Niaw Look Pueng 11.45 ± 0.03 1.5 ± 0.07 2.37 ± 0.06 7.16 ± 0.01 3.17 ± 0.84 77.53 ± 0.01 360.06 ± 0.49
Sung YodPhatthalung 9.28 ± 0.06 1.42 ± 0.12 2.67 ± 0.06 10.36 ± 0.04 4.51 ± 1.60 76.27 ± 0.13 370.53 ± 0.95
NiawDawk Yong 12.01 ± 0.01 1.45 ± 0.06 3.19 ± 0.06 9.62 ± 0.16 3.75 ± 0.79 73.73 ± 0.10 362.10 ± 0.26
Niaw Lan Tan 13.12 ± 0.16 1.26 ± 0.05 3.08 ± 0.08 7.35 ± 0.06 3.27 ± 1.20 75.20 ± 0.16 357.86 ± 0.37
Sri Lanka Red Rice 1 12.94 ± 0.03 0.82 ± 0.14 1.15 ± 0.03 9.63 ± 0.04 2.82 ± 0.55 75.45 ± 0.09 350.72 ± 0.42
China Red Rice 11.90 ± 0.20 1.37 ± 0.02 2.35 ± 0.03 9.72 ± 0.04 2.52 ± 0.24 76.66 ± 0.17 358.72 ± 0.82
Black
Niaw Dam Pleuak Khao 12.59 ± 0.16 1.42 ± 0.01 3.72 ± 0.06 8.17 ± 0.41 4.01 ± 0.58 74.09 ± 0.48 362.55 ± 0.85
Niaw Dam Pleuak Dam 12.03 ± 0.13 1.48 ± 0.02 3.65 ± 0.05 10.85 ± 0.09 3.41 ± 0.24 71.99 ± 0.08 364.22 ± 0.79
China Black Rice 11.26 ± 0.28 1.74 ± 0.02 2.85 ± 0.09 8.44 ± 0.02 4.08 ± 0.54 75.71 ± 0.37 362.25 ± 0.96
Source: [4].
FOOD REVIEWS INTERNATIONAL
5
different amount of total protein content 7.4–11.3 g/100 g,[29] 7.16–10.85 g/100 g[4] in
different varieties of rice and this significant difference among protein content of various
rice varieties are possibly due to environmental factors, nitrogen fertilizers, genetic traits
and production system.[30] Wei et al.[31] reported that the total protein of the seven
different rice cultivars determined by the Bradford method was found to be in the range
of 87.9–92,7 mg/g dry weight, while these values were significantly higher than those
obtained using Kjeldahl method (58.2–73.74 mg/g dry weight) as presented in Table 2.
The differences in values obtained from the two methods may be due to the coomassie
brilliant blue staining in Bradford method or the interference of SDS used in the extrac-
tion buffer with protein staining in Bradford method, the other possible reason might be
the interaction between protein and dyestuff.[31] The protein content in rice varies with
the geographical location. Verma & Srivastav[7] studied the six aromatic and two non-
aromatic rice accessions procured from the different parts of India and reported that the
protein content of the rice accessions is in the range of 7.74–10.72% (Table 3).
Rice seed protein classification

Osborne,[8] classified proteins on the basis of their solubility in various solvents such as
water, salt solution and alcohol or weak acid/alkali solution. Osborne classified proteins
like albumin (water soluble), globulins (soluble in salt solution), prolamins (alcohol
soluble) and glutelins (soluble in weak acid/alkali solution). Rice seed storage proteins
are unique amongst cereal proteins, as most cereals have prolamin as their major storage
protein; however, rice is richer in other fractions and has a lower prolamin content.[33,34]
Rice proteins, specifically in the bran that is rich in albumins and globulins comprises of
proteins that possess good antigenic activity.[35] Rice proteins are easily digestible (73.0%)
and so are absorbable with a net protein utilization (NPU) of 73.8 as compared to wheat
(53.0), corn (58.0), barley (62), and millet (56.0). Protein efficiency ratio ranges from 1.6 to
1.9; however, it increases to 2.0–2.5 in protein isolates and concentrates, which is equiva-
lent to casein.[36,37] They are also rich in the essential amino acid lysine in comparison
with other cereal proteins.
Rice seed protein is present as protein bodies in the grain; two main protein bodies PB-
I & PB-II are present in the grain endosperm. The sub-aleurone layer possesses a greater
quantity of these bodies followed by the central region, no protein bodies were visualised
in the aleurone cells. The protein bodies PB-I & PB-II differs in structure & composition.
Table 2. Amount of total protein and low molecular weight proteins (mg/g dry weight).
Total protein Albumin
Cultivar Bradford Kjeldahl +Globulin Prolamin
Ilmibyu 90.8 ± 1.3ab 58.22 ± 0.01a 10.70 ± 0.27ab 1.31 ± 0.01a
Ilpumbyu 95.7 ± 1.3 c 63.20 ± 0.04 c 11.98 ± 0.21b 1.80 ± 0.11b
Saechuchungbyu 92.6 ± 1.6bc 72.35 ± 0.07 f 11.08 ± 0.49bc 2.20 ± 0.08 c
Chuchungbyu 87.9 ± 1.1a 61.12 ± 0.01b 9.94 ± 0.39a 1.64 ± 0.04b
Junambyu 89.9 ± 1.2ab 66.91 ± 0.06e 11.65 ± 0.76bc 1.85 ± 0.10b
Dongjinbyu 91.7 ± 1.6b 64.71 ± 0.01d 10.54 ± 0.62ab 1.60 ± 0.17b
Nampyungbyu 92.7 ± 3.4bc 73.74 ± 0.10 f 11.10 ± 0.40bc 1.84 ± 0.21b
Data are expressed as mean ± standard deviation (n = 3). Difference letters in the same column indicate significant
differences (p < 0.05). Low molecular proteins such as albumin, globulin and prolamin were analyzed by fractionation.
Source: [31].
Table 3. Protein content and distribution of protein fractions in 12 varieties of rice grown in North
Vietnam.
Total protein recovered
Glutelin
Cultivar Protein content (N × 5.95) Albumin (%) Globulin (%) Prolamin (%) (%)
Tam 10.50 7.00 10.90 8.60 73.50
Du 9.20 8.80 9.40 7.80 74.00
Gie 8.80 10.50 8.30 7.60 73.60
Sai Duong 10.60 4.00 12.50 6.40 77.10
Nep Mua 10.80 8.20 10.50 6.00 75.30
Bau Chau Qui 9.70 7.10 7.60 6.50 78.80
Cuom Chau Qui 8.70 6.20 10.20 7.90 75.70
Tran Chau Lun 9.60 5.90 8.30 8.10 77.70
NN5 7.80 5.40 9.00 7.00 78.60
NN8 8.90 5.80 6.00 8.20 80.00
NN756 7.00 7.40 7.10 5.50 80.00
NR2151 10.60 8.90 11.20 9.50 70.40
Average 9.35 7.11 9.35 7.34 76.23
Source: [32].
PB-I accounts for prolamin and has a spherical lamellar structure; PB-II has no lamellar
structure and is devoid of prolamin subunits, glutelin and globulin are the main compo-
nents of PB-II.[9]All rice bran products including proteins are reported as nontoxic by
various researches and panels such as the Cosmetic Ingredient Review (CIR) expert
panel.[38]
The protein fractions in rice seed are heterogeneous in nature, this could be attributed
to cultivar differences and method of protein extraction used.[39] The distribution of
protein fractions and thus total protein content in rice flour are different compared to
bran. Studies by Ju et al.[40] have reported that flour contains 4.5%, 13.1%, 79.7% and 2.6%
of albumin, globulin, glutelin and prolamin, respectively.
Fractional weights
Adebiyi et al.[41] reported that the molecular masses of albumin, globulin, glutelin and
prolamin fractions were distributed in the range of 30–45, 20–66, 10–66 and 10–53 kDa,
respectively, whereas earlier studies conducted by Hamada,[42] resulted in different values,
their research arrived on rice bran albumin, globulin, glutelin and prolamin to be in the
range 10–100, 10–150, 33–150, and 25–100 kDa, respectively. A similar study by
Amagliani et al.[43] showed that rice albumin was resolved into a wide range of subunits,
with molecular weight (MW) ranging from about 13 to 110 kDa. Shibuya & Iwasaki,[44]
reported Albumin to be between 10 – 200 kDa and globulin to be between 16 and 130
kDa. Various other studies on rice bran and flour protein also report different relative
molecular mass values for the various protein fractions, these discrepancies are assumed to
be caused by the heterogeneous nature of polypeptides in rice flour and bran.
Albumin
Albumin constitutes 4% to 6% of seed protein in rice, around 35% of rice bran, 4% to 8%
of the endosperm and is a minor protein type along with prolamin.[41] Albumin content in
bran is seen to be nearly 6 times greater as compared to normal rice, with albumin
yielding eight peptides upon hydrolysis.[45] Digesting rice albumin with trypsin shows the
presence of 24 peptides whereas 28 are predicted from its amino acid composition. It is
seen to possess a major glycoprotein fraction that is a 60 kDa monomer with an isoelectric
point of 6.54.[46] The relative molecular mass values determined by size-exclusion HPLC
were 10–100 kDa[42] however the same was reported to range from 10 to 200 kDa in an
earlier study by Shibuya & Iwasaki,[44] using conventional size-exclusion chromatography.
Albumins are generally extracted by solubilising them with distilled water (400–600 mL)
by shaking or stirring and subjecting it to centrifugation (3500–4000 g for 15 min.) to
allow its separation. They are water soluble and coagulate upon heating like albumins of
other cereals, possessing minimal disulphide cross links and sufficient net charge. They
have been cited to possess appreciable antigenic properties.[35] Ju et al.[40] reported that
their studies yielded 97% protein extraction out of which albumin’s share was reported to
be 4.5% with an Isoelectric pH of 4.1 and enthalpy of 2.88 J/g. Denaturation temperatures
for albumin were reported to be 75.7 degrees and 73 degrees by Ju et al.,[40] and Adebiyi
et al.,[41] respectively.
Albumin hydrolysates are also found to exhibit the highest Angiotensin-converting
enzyme (ACE) inhibiting activity amongst the rice protein fractions, thus possessing high
nutraceutical utility by aiding in the relief of hypertension.[16,47] Functional bioactive
peptides and compounds have been derived from albumin proteins, peptide compounds
such as “oryzatensin” obtained from the ‘RA5ʹ fraction of albumin show bio-regulatory
activity in the human gut by influencing contraction of the ileum.[48] Trypsin hydrolysed
denatured albumin (MW 800 to 2100Da) shows high antioxidant activity, surpassing the
activity of its native Rice Bran Protein (RBP) and hydrolysate forms.[49] Albumin proteins
also hold the minimal allergenic proteins found in rice, such as the 14–16 kDa protein that
inhibits serum IgE binding activity which is seen in the endosperm albumin, these hail
from the wheat α-amylase-trypsin inhibitor family.[50] However, these have not been
observed in RBPs and this may be attributed to the fact that rice bran proteins would
undergo structural disintegration/denaturation during the extraction process that gener-
ally employs alkaline solvents and enzymes. Albumins also possess the highest phytate
content amongst the four, which can act as an anti-nutritional factor that must be
removed before usage in food formulations
Globulin
Globulins are salt soluble proteins and are the second most abundant rice seed protein
fraction. They possess good antigenic properties[35] and have an isoelectric point of 4.3. It is
extracted by solubilizing it with NaCl (400 mL to 500 mL for 3 to 4 h) and centrifuging at
4000 g for 15 to 20 min.[41] Globulin fractions are seen to have molecular weights of 10–150
kDa.[42] They are found in crystalline Protein Bodies that range from 2–3 μm in diameter.
Most of these can be seen in the sub-aleurone layer.[9] It is predominantly found in rice bran
and polish and accounts for 8–10% of total endosperm proteins.[37] The globulin fraction is
characterized by its lack of aggregation, rice globulins are argued to be made of polypeptide
chains of different sizes linked by inter-chain disulphide bonds.[42] Adebiyi et al.[41] reported
that Rice globulin is seen to possess a structure similar to oat globulin, its solubility
characteristics are seen to be influenced by the presence of random coil structure, anti-
parallel chain of intra-molecular β-sheet structure which is absent in albumin. Globulin also
seems to have a relatively low denaturation temperature of 60 degrees. The rice globulin
fraction is composed of two polypeptides of 23–27 kDa and 16 kDa.[51] The 23–27kDa
polypeptides, termed a-globulin, is structurally homologous to wheat grain glutenin.[52]
Table 4. Protein content of rice bran reported in past studies.

References Albumin Globulin Prolamin Glutelin
Cagampang et al.[53] 37% 36% 5% 22%
Betschart et al.[54] 40% 21% 3% 36%
Hamada[42] 34% 15% 6% 11%
Adebiyi et al.[41] 37% 31% 2% 27%
Chanput et al.[55] 30.9% 24.9% 11.6% 32.6%
Globulin contains the highest amount of the sulphur-containing amino acids cysteine and
methionine but has a lower level of lysine content as compared to albumin and globulin.
Hamada[42] had earlier reported that cultivars do not contribute to a significant differ-
ence in the amount of globulin proteins that are extracted from bran. More recent studies
(shown in Table 4) however show high discrepancy and they attribute this difference to
both the extraction methods used and the cultivar taken for the study. Spectroscopic
studies conducted on rice globulin show that it exists as predominantly α-helical struc-
tures, and is influenced by pH, ionic strength, by some protein structure perturbants and
heat treatments. Covalent and non-covalent forces are seen to be involved in protein
stabilization while hydrophobic and disulphide interactions influence aggregation upon
heating.[51]
Glutelin
Glutelins are the alkali-soluble protein fraction of rice seed; they are made of two subunits
with molecular weights of 30–35 kDa (α) and 19–25 kDa (β) respectively. Glutelins are
generally considered the primary seed storage protein present in rice unlike other cereals
where prolamin holds this value. It is poorly soluble in water but is readily solubilizes in
alkali and acidic conditions (pH >10 and pH <4, respectively). The hydrophobicity of
insoluble glutelins may be decreased by use of several dissociating agents such as sodium
dodecyl sulfate (SDS), sodium stearate, and cetyltrimethylammonium bromide or other
surfactants.[42] The bran and endosperm are argued to contain 11–27% and 66–78%,
respectively.[56,57] It is mainly found in Protein Body II (PB II) and contains a good
amount of lysine, just behind rice albumin. The molecular mass peak was observed at
a range of 11–52 kDa when analysed using MALDI-TOF mass spectrometry.[41]
The presence of Glutelin as the major protein fraction makes it highly suited towards
alkaline extraction. Dilute alkali solvents like 0.1 M NaOH or 0.1 M KOH are employed to
extract the glutelin fraction out, most food industries, however, employ this method to
obtain purified rice starch. They are also strongly aggregated with disulfide linkages.
Glutelin is said to be present at around 75–81%, 79–83% and 22–45%, in brown rice,
milled rice and rice bran, respectively.[43] Ju et al.[40] reports that glutelin has an Isoelectric
pH of 4.8, which they determined by measuring the supernatant’s turbidity post extraction
from defatted rice flour. Chrastil and Zarins[58] have reported that purified glutelin
subunits, the α (acidic) and β (basic) polypeptides can be segregated into 9 and 5 bands,
respectively, with isoelectric pH of 5.0–8.0 and 8.0–11, respectively.
Prolamin
Prolamins are alcohol soluble protein fractions. They are a minor protein fraction in rice
seed, made of heterogeneous polypeptides that are more evenly distributed across the rice
fractions compared to other proteins. Prolamins constitute 2.6–3.3% & about 4% of

protein in rice endosperm and bran, respectively.[53,59] They are the hydrophobic protein
fractions localized in protein bodies I (PBI). They are generally extracted by ethanol-water
mixtures, 70% propanol is seen to be a much better extraction solvent for the same.[60] Its
relative molecular mass lies from 33 to 150 kDa with the majority concentrated around
105 kDa.[42] Prolamin present in supernatant post centrifugation was shown not to
aggregate on pH but acetone is seen to precipitate out the fraction. It seems not to
show any thermo-graphic denaturation peak when analysed by DSC.[40] Prolamin fraction
had a high-intensity major peak at 19 kDa when analysed using MALDI-TOF mass
spectrometry.[41] Three polypeptide subunits with apparent MWs of 10, 13 and 16 kDa
were identified.[61] The 13 kDa polypeptide is the major prolamin fraction and is char-
acterized by high glutamine, arginine, glycine & alanine, but lower sulphur-containing
amino acids, the 16 kDa and 10 kDa fractions contain greater amounts of methionine and
other sulphur amino acids.[62]
Amino acid composition

The amino acid profile of the food product is very important in the nutritional point of
view and also relates to the physical and chemical properties of the food product.[12,63,64]
The content of essential amino acids such as methionine and phenylalanine is higher in
rice protein isolate as compared to casein and also rice protein isolate contains higher
amount of leucine, methionine and threonine than the soya protein isolate. As shown in
Table 5, RPI contains higher amount of essential amino acids such as histidine, methio-
nine, and phenylalanine as compared to fenugreek protein isolate, so the combination of
rice protein isolate with any of the three casein, soya protein isolate or fenugreek protein
isolate in the food formulation might result in good protein source.[10–12]
Rice protein contains all the essential amino acids as shown in Table 6. According to
Wei et al.[31] and Khoi et al.,[32] rice protein contains histidine (1.0–3.8%), threonine
(3.15–4.43%), valine (5.0–7.31%), methionine (0.8–1.77%), phenylalanine (1.18–5.81%),
isoleucine (3.60–5.35%), leucine (6.90–8.82%), and lysine (1.3–5.10%).
Rice protein extraction methods

The functional and physicochemical properties of extracted rice seed protein greatly
depend on the extraction method used. Various conventional and novel methods have
been explored by researchers to achieve high yield and minimal effect on protein proper-
ties. Several protein extraction methods have been developed and optimized by various
researchers till date, and are discussed below.
Alkali extraction
Alkali extraction method is the most widely used method of protein extraction. The
proteins are exposed to alkali for dissolving the protein in the preparation of protein
isolate/concentrate.[65] Nashef et al.[66] reported that disulfide containing proteins having
different properties and structures when treated with alkali resulted in similar types of
products but possessing different activation energies. The extreme pH condition during
alkali extraction process changes the native structure of the proteins and also affects the
Table 5. Amino acid composition of various protein sources.

RPI Casein FPI
Amino acids (%) CRBP (g/100 g protein) (%) SPI (g/100 gm protein) (g kg−1)
Essential amino acid
Histidine 2.05 3.39 2.25 2.54 16.0
Threonine 4.17 3.49 4.59 3.71 80.01
Valine 2.34 5.41 5.77 4.80 54.70
Methionine 4.62 2.05 2.10 1.10 7.70
Phenylalanine 4.49 6.80 3.46 5.41 23.90
Isoleucine 2.07 3.23 3.54 4.93 59.70
Leucine 4.55 7.34 6.41 1.72 93.70
Lysine 3.41 5.82 8.48 6.09 51.70
Non-essential amino acids
Tyrosine 3.87 4.07 3.51 3.70 37.00
Cysteine - 2.21 - 1.01 7.40
Aspartic acid 11.44 9.22 9.17 11.96 116.80
Glutamic acid 17.82 15.47 18.80 20.53 199.80
Serine 9.49 4.69 7.99 5.51 27.50
Glycine 8.44 4.20 4.99 4.64 46.00
Arginine 7.84 9.03 3.23 7.81 75.70
Alanine 6.73 6.11 4.99 3.90 35.70
Proline 6.67 3.81 12.40 5.28 9.70
Percentage of amino acids with different characterization
Basic - - - 160.40 143.40
Acidic - - - 278.80 316.60
Hydrophobic - - - 314.10 285.10
Uncharged polar - - - 168.00 197.91
Charged polar - - - 439.00 460.00
Sulfur-containing - - - 31.60 15.10
Basic: lysine, arginine, histidine; acidic: aspartic acid, glutamic acid; hydrophobic: alanine, isoleucine. Leucine, methionine,
phenylalanine, valine, proline; uncharged polar: glycine, serine, tyrosine, cysteine, threonine; charged polar: basic and
acidic amino acids; sulfur-containing: cysteine, methionine.
Source: [10,11,13].
nutritional value of the protein. De Groot & Slump[65] studied the severe alkali treatment
on the nutrition value and amino acids composition of proteins and reported the
destruction of cystine and lysine amino acids. Lysine is the limiting amino acid in the
rice proteins therefore alkali extraction method should be used at optimum conditions to
prevent the loss of nutritive value of protein. Paraman et al.,[67] in his research, optimized
the alkali extraction condition of the rice protein with 65.9% yield and 86.9% protein
content. For protein extraction, a suspension of one kg of rice flour in 8 L of de-ionized
water was prepared and homogenized for 5 min. The pH of the suspension was adjusted
to 11 by 1 M NaOH solution and stirred for 3 h at 40° C. The solution was centrifuged for
15 min at 3840 × g to separate the solubilised protein; the supernatant was collected
separately while the same procedure was repeated on the residue to extract the additional
protein. The pH of the supernatant collected was adjusted to the iso-electric pH (4.5) to
precipitate the protein. After pH adjustment, the solution was kept undisturbed for 1 h at
4° C and protein precipitate was recovered by centrifugation for 20 min at 5000 × g. The
de-ionized water (pH 4.5) in w/v ratio of 1:4 was used for washing of protein precipitate.
The pH of the protein precipitate thus obtained was adjusted to 7.0, followed by freeze
drying and storage at 5°C.[67]
12
Table 6. Amino acid composition of various rice cultivars.

N. GHANGHAS ET AL.
Cultivars
Amino acids Keu Nak Ohd Wha Tam Du Gie SD NM BCQ CCQ TCL NN5 NN8 NN 176 IR-2151
Cys 3.60 2.80 2.70 3.20 1.00 1.40 2.40 2.00 1.40 1.12 1.89 1.37 2.22 2.31 1.85 2.01
Asp 10.00 9.60 9.80 10.40 8.00 9.20 9.00 10.20 8.67 9.15 8.75 9.00 7.80 8.06 8.75 9.86
Glu 26.60 26.70 26.40 27.00 20.00 15.00 21.10 16.00 17.15 19.33 17.21 18.00 16.40 19.21 16.65 18.20
Ser 5.40 5.80 5.60 5.60 3.00 3.60 5.90 5.90 6.00 3.99 4.50 3.00 5.50 5.15 6.00 6.18
Gly 5.80 4.90 4.60 4.40 4.50 4.90 4.33 5.00 4.65 4.00 4.80 4.01 4.33 4.27 4.85 4.66
His 3.50 3.40 3.80 3.60 1.00 1.80 2.50 2.00 1.46 1.79 1.80 1.38 2.05 2.44 1.95 2.05
Arg 3.90 3.80 4.00 3.80 7.20 8.15 9.30 8.77 8.25 7.11 9.00 8.66 8.25 7.21 8.11 7.85
Thr 4.10 4.20 4.10 3.90 3.40 3.48 4.43 4.00 3.37 3.15 4.01 4.00 3.35 3.15 3.67 4.02
Ala 5.00 5.50 5.80 5.80 4.50 5.11 6.50 6.01 6.02 4.80 5.33 4.61 5.00 5.11 4.99 5.77
Pro 8.80 7.90 7.20 6.60 3.00 3.90 4.33 6.90 4.00 3.77 4.15 4.22 3.81 3.00 4.15 3.47
Tyr 0.30 0.30 0.20 0.20 4.50 4.00 3.60 4.12 4.70 3.80 5.01 4.30 3.99 4.33 3.03 4.11
Val 6.10 6.50 6.70 6.50 5.30 5.70 5.76 7.00 7.30 5.22 6.15 5.00 6.28 6.90 5.11 5.38
Met 0.80 1.50 1.30 1.20 1.40 1.03 1.77 1.60 1.35 1.58 1.38 1.19 1.61 1.39 1.47 1.42
Ile 3.60 3.70 3.90 3.90 5.40 4.25 5.00 4.82 4.54 4.15 5.35 4.84 4.10 4.29 5.10 5.01
Leu 6.90 7.50 7.70 7.90 8.82 8.67 8.19 8.40 8.71 8.00 8.63 8.75 8.57 8.65 8.00 8.32
Phe 4.30 3.90 4.10 4.10 4.00 4.73 5.01 5.81 4.60 1.18 4.35 5.00 4.15 5.11 4.33 4.22
Trp 0.00 0.30 0.20 0.20 1.00 1.61 1.52 1.70 1.72 1.18 1.37 1.31 1.62 1.12 1.33 1.34
Lys 1.30 1.60 1.80 1.70 4.30 4.67 4.95 3.39 4.71 3.10 3.95 4.17 3.80 4.00 5.10 4.25
Keu: Keumhobyu; Nak: Nakdongbyu; Ohd: Ohdaebyu; Wha: Whaseongbyu; SD: Sai Duong; NM: Nep Mua; BCQ: Bau Chau Qui; CCQ: Cuom Chau Qui; TCL: Tran Chau Lun. Source: [31].
Ultrasonic assisted alkali extraction

Ultrasound is a non-thermal physical processing technology that has gained attention for
its application in extraction of various bioactive substances from food matrix.[68,69]
Ultrasound produces acoustic cavitation in liquid that facilitates the extraction process
by disruption of cell walls and membrane. Acoustic streaming generated in liquids by
ultrasound results in the rapid formation and collapsing of gas bubbles, that results in
production of high shear and mechanical energy, which ruptures cell walls and
membrane.[70,71] This facilitates the penetration of solvent into cellular material, improves
mass transfer, and better release of extract.[69] Ultrasound-assisted extraction process has
advantages as it avoids high-temperature hydrothermal effects which prevent the protein
denaturation and loss of functionality, requires moderate amounts of solvent, and reduces
extraction time.[70,71]
Ultrasound-assisted alkali extraction involve the combination of alkali and ultrasound
treatment to extract protein. In this method, a rice bran suspension is prepared in distilled
water in 1:5 ratios, in a conical stainless steel container and kept in ice bath to control the
temperature. The pH of the suspension is adjusted to 11 and ultra-sonication treatment is
applied at 100 W for 5 min using ultrasonic generator (cycle of 59 s ON and 10 s OFF).
The pH was re-adjusted after 2.5 min. After ultrasonic treatment, the further steps were
similar to conventional method off alkali method, which includes removal of insoluble
material by centrifugation, filtration, isoelectric precipitation by adjusting pH at 4.5, again
centrifugation, washing, freeze drying and storage below 40°C.[72]
Extraction by fractionation method

Fractionation method of protein extraction is based on the Osborne classification of
proteins. The fractionation method is of great advantage as compared to other methods
as it results in individual separate fraction of protein. This is easy and reliable method to
get separate individual fraction of protein and is of great help when the interest of
researcher is to study the different protein fractions.
This method was described by Ju et al.[40] in their research, they extracted rice flour
protein and studied its properties. For protein extraction, 100 g of rice flour was defatted
using 400 ml of hexane and air dried for 24 h. The different protein fractions were
extracted in four steps (water extract, salt extract, alkali extract, and alcohol extract)
from the defatted rice flour. The albumin fraction was first extracted using water as
solvent; defatted rice flour was mixed with 400 mL distilled water (20° C) and shaken
for 4 h followed by centrifugation for 30 min at 3000 × g. The supernatant containing
dissolved albumin was collected separately, while the residue was mixed with 400 mL of
5% NaCl solution and stirred for 4 h to extract globulin fraction of protein. The solution
was again centrifuged for 30 min at 3000 × g and the supernatant containing dissolved
globulin was collected separately. The glutelin fraction was extracted from the residue
obtained from the previous step by alkali extraction method; the residue was mixed with
300 mL of water and pH was adjusted to 11.0 using 0.02 M NaOH (20° C), stirred for 30
min to dissolve glutelin fraction of protein. The supernatant obtained after centrifugation
at 3000 × g for 30 min was collected separately, while the residue was used for extraction
of prolamin. The residue was mixed with 300 mL of 70% ethanol and was shaken for 4 hr
at 20° C. The protein fractions were precipitated by adjusting the pH of supernatant to the
iso-electric point of each protein fraction, except prolamin which was precipitated by
acetone. The iso-electric pH determined by Ju et al.,[40] using turbidity measurement and
reported that albumin and glutelin precipitate at pH 4.1 and 4.8, respectively, while
globulin precipitate at both 4.3 and 7.9 pH. After the precipitation, proteins were washed
twice by distilled water and freeze dried after adjustment of pH to 7.0.[40]
Enzymatic extraction method

The major component of rice flour is starch, for protein separation hydrolysis and
solubilization of starch is done using α-amylase enzyme. According to Shih et al.,[73] the
use of carbohydrate hydrolyzing enzymes such as cellulase or combination of cellulase and
hemicellulase in addition to the α-Amylase enriches the protein in the residue. For
enzymatic extraction of protein, slurry of rice flour is prepared by adding 6 L of de-
ionized water to 1 kg of rice flour and is stirred at 60°C for 15 min followed by treatment
with 0.5% Termamyl. The temperature is increased gradually to 90°C and incubated for 2
h at 90°C to hydrolyze and solubilize the starch. The supernatant containing solubilized
starch is removed by centrifugation for 15 min at 3840 × g. The residue solid was mixed
with de-ionized water (3 L) and is incubated at 50°C with 0.1% cellulase for 30 min. Now
the pH is reduced to 4.5 at 90°C to inactivate the enzymes and centrifuged to remove
dissolved cellulose fraction. The protein precipitate thus obtained is washed twice with
warm deionized water followed by pH adjustment to 7.0. The protein solution is freeze
dried and stored at 5°C after freeze drying.[67]
Enzyme-assisted micro-fluidization
Xia et al.[74] reported that rice protein can be effectively extracted from broken rice by
applying micro-fluidization treatment to wet-milled broken rice, followed by density-based
separation. Microfluidization treatment disrupts the protein-starch agglomerate, and further
enzyme treatment removes the starch residue and increases protein purity. In this method,
distilled water is added to broken rice in solid to solvent ratio of 1:20 (w/v) and colloid
milled (wet milling) for 30 min. After colloid milling, the slurry is processed by two pass
microfluidization at 100 MPa. This is carried out to disrupt the protein-starch agglomerate.
The microfluidized slurry was centrifuged for 10 min at 8000 × g, followed by decantation of
the supernatant thus obtained. Two different layers, one rich in protein and the other in
starch were observed in the precipitate due to their difference in density. The supernatant
protein layer was scrapped cautiously and re-dispersed with 10 times (w/v) distilled
water.[74] For increasing the purity of the protein-rich fraction enzymatic method was
employed as discussed in previous section.
Functional properties of rice seed protein

Increasing global demand for new sources of food proteins led to the incorporation of
vegetable proteins in foods to produce novel foods. Plant source of proteins are abundant
and relatively inexpensive with higher nutritive value and excellent functional properties.
Functional properties of the food ingredients are those properties on which the utility of
those foods depends. The functional properties depend on various factors such as extrac-
tion method used, treatment employed, food pH, concentration of salt & sugar in the
foods, and also on the other components present in the food such as carbohydrates &
lipids.[13,14]
Solubility
Rice protein isolate has a very low solubility in the pH range of 3 to 9 and above pH 9 it
shows a slight increase in solubility.[11] According to Romero et al.,[75] rice protein
concentrate shows poor solubility (25–55%) over a wide range of pH (2 to 10) and
minimum solubility at iso-electric point (pH 4.5). Glutelin is a high molecular weight
protein and it is composed of subunits which are bound by the di-sulphide linkages
therefore it is soluble only in dilute acid or alkali. The high percentage of glutelin fraction
(about 80%) of rice protein results in the low solubility of the rice protein isolate. Shih &
Daigle[11] described that rice protein alone shows very limited solubility in water but
shows significant increase in the solubility in the presence of xanthan gum. The portion of
rice seed from which the protein is extracted significantly effects the solubility. In the pH
4–7 the Rice Bran Protein solubility is higher than brown rice protein and white rice
protein while at the pH value >7 or <4, solubility of white rice protein is reported to be
higher than brown rice protein and rice bran protein.[76] This difference in solubility is
due to the Glutelin which is the major component of the protein extracted from both
Brown Rice and White Rice. Solubility of rice protein is one of the limiting factors for its
application in food. Wang et al.[12] reported solubility of rice protein increases signifi-
cantly compared to the control sample when rice protein is freeze milled. According to
Wang et al.,[12] freeze milling exerts a profound mechanical energy on the Rice Protein
which results in the unfolding of the rice protein. The unfolded conformation exposes the
functional groups to the solvent and this strengthens the interactions of water and protein.
Pietrysiak et al.[77] used direct steam injection (DSI) process to exploit the potential
application of pea rice (PR) protein isolate blend and reported significant increase in
the solubility of DSI-PR. Solubility of PR control sample was <4% while the solubility DSI-
PR at pH 3, 6, 9 were <14%, 14.9% and 50.1%, respectively.
Foaming properties
Foaming property of proteins is crucial in the production of different types of foods.
Foams are two-phase system having air cells separated by a continuous liquid layer. For
application in a variety of foods, proteins should form stable foams effectively and rapidly
over the pH range of the food and also at low concentration.[78] According to Tang
et al.,[79] as a prerequisite to have foam capacity, the proteins should solubilize in the
aqueous phase and rapidly unfold to form a cohesive layer of protein around gas/air
droplets. Diffusion, rapid changes in the conformation and succeeding rearrangement at
air–water interface is crucial to obtain protein-based foams[12] and for this, flexible protein
molecules with few secondary and tertiary structures are required[79] and for the devel-
opment of stable foam, the formation of continuous intermolecular polymer of protein
molecules around the air bubbles is important. This is because stable foam formation
requires this intermolecular cohesiveness and elasticity.[79] The foaming capacity (FC)
depends on the pH, salt concentration, and sucrose concentration. The increase of the pH
from 5 to 11 has resulted in 3.65-, 5.52-, and 4.21-fold increase in the FC of brown rice
protein, white rice protein and rice bran, respectively. The FC of BRP, RBP and WRP
remains unaffected up to 12% sucrose concentration but above 12% FC declines signifi-
cantly (P < .05). The increase in salt concentration from 0.4% to 2%, significant (P < .01)
increase in FC of Rice Bran Protein was reported, while for the Brown Rice Protein and
White Rice Protein, the foam only significantly (P < .05) increased at low salt concentra-
tion and above 0.8% FC remains constant.[76] Khan et al.[80] reported that un-stabilized
rice bran protein isolate (Un-PI) forms relatively dense and stable foams as compared to
microwave stabilized rice bran protein isolate (MW-PI), dry heat stabilized rice bran
protein isolate (DH-PI) and parboiled rice bran protein isolate (PAR-PI). Foaming
capacity and foaming stability are maximum for Un-PI (15.7 mL, 84 min) followed by
MW-PI (10.5 mL, 74 min), DH-PI (10.4 mL, 71 min) and PAR-PI (9.2 mL, 56 min).[80]
Chandi and Sogi[81] reported FC of rice bran protein concentrate (RBPC) extracted from
HBC 19 rice cultivar (5.2%) is higher than the casein (3.95%) at pH 5 and at neutral pH,
the FC of both casein (14.25%) and RBPC of HBC 19 (8.10%) has increased. The FC of
Casein decreased to 10.15% while FC of RBPC of HBC 19 increased to 10.03% when the
pH was shifted from 7 to 9. The possible reason for the lower FC at acidic pH might be the
isoelectric point (pH 4.5) of the rice bran protein.
Emulsifying properties
Emulsification properties are defined in terms of emulsifying activity index, emulsifying
capacity and emulsifying stability, and these properties are crucial for food applications
such as the development of various traditional and novel foods. Although the main
emulsifying agents are proteins, but its emulsifying activity within the food can alter
due to the presence of carbohydrates and might result in the change in quality of
food.[82,83] Proteins and other amphoteric molecules facilitate the formation of stable oil
droplets through the development of interfacial membranes and improve the oil droplet
dispersion in the immiscible phase of the emulsion by preventing the coalescence of
droplets.[82] Emulsifying activity index is defined as the protein’s ability to induce creation
of the newly formed dispersed particles in emulsions, whereas emulsion capacity denotes
the maximum amount of oil that is emulsified by standard amount of protein under
specific conditions. Emulsifying stability is measured as the amount of cream/oil separated
from emulsion during a specific period of time at definite temperature and gravitational
field.[78,83] Emulsion formation depends on various factors such as homogenizer type,
degree of homogenization, volume fraction of oil, pH, and volume of dispersion, type of
oil and also on the starch incorporated into the food.[82,83] Cao et al.[76] studied three types
of rice proteins, i.e. brown rice protein, white rice protein, and rice bran protein at
different conditions of pH, salt and sugar and reported that the white rice protein has
18.52% higher emulsion capacity at pH 3–11 than that of rice bran protein. At pH 11, the
three types of rice protein – brown rice protein, white rice protein and rice bran protein
showed maximum emulsifying volume of 44.32%, 47.06%, and 42.93%, respectively.
According to Cao et al.,[76] white rice protein (mainly glutelin) is a better emulsifier
than the other two types of rice protein in strong acidic and alkali conditions because of
the improvement in protein solubility due to the breakdown of disulphide bonds. The low
hydrophobicity of protein results in the decrease in emulsifying properties of protein as it

will not facilitate protein and oil interaction. Cao et al.[76] reported that with the increase
in the NaCl concentration significantly (p < .05) reduced the emulsifying capacity of
proteins because NaCl reduced charge adsorption at interfaces of protein. Also, at the 4%
sugar concentration, all the three types of protein have shown maximum emulsification
while it decreased with the further increase in the sugar concentration. Rice bran protein
showed higher emulsification than other two in both salt and sugar solution, this might be
due to the higher hydrophobic amino acids content in rice bran protein than white rice
protein which improves its surface hydrophobicity. The protein and lipid interaction
increase with the exposure of more hydrophobic groups.[76]
Water absorption
Water-absorption capacity and water-holding capacity determine the ability of a food
product to imbibe and hold water in its matrix. This property is especially important to
food substances that need high water retention; baked foods rely on high water absorption
capacity to minimize moisture loss post packaging. WAC also maintains freshness, overall
product mouth feel and texture.[81] Water absorption capacities are generally determined
by dissolving 0.5–1 g of the protein in 5–10 mL of distilled water, allowing it to rest,
centrifuging at around 3000 g and measuring the volume of the supernatant.[84] Chandi &
Sogi[81] carried out water absorption studies of Rice bran protein concentrates from
various rice varieties including Basmati and found them to have good WAC enabling its
usage in products that need high water retention. Their studies also showed that water
absorption and Nitrogen solubility index of proteins are related in some manner, casein
with the lowest Nitrogen solubility index is seen to have the least water solubility.
Parboiling has a negative impact on water absorption, supposedly due to conformational
changes induced by processing.
Zhau et al.[85] reports that the water holding capacity of rice endosperm protein and
rice dreg protein are 2.81 g/g and 3.02 g/g, respectively, these values are lower than that of
Soy protein isolates but however are well under the values stated by Aletor et al.[86] as
recommended for viscous foods. Cao et al.[76] have also outlined in their studies that
Brown Rice Protein and White Rice Protein have low water-binding values of 1.96 and
1.78 mL/g, respectively, followed by Rice Bran Protein with (3.54 mL/g). Water absorption
in the range of 1.49–4.72 g/g is deemed as essential for viscous food systems like gravies,
curries and soups,[86] thus rice protein is seen as a component that can surely serve the
purpose of water retention in recipes. Rice bran protein, in particular, can be used as an
ingredient for achieving the same.
Oil absorption capacity

Oil absorption capacity (OAC) of proteins is essential in order to improve mouth feel and
flavour retention of certain food products.[84] Oil absorption is generally found by mixing
0.5–1 g of protein with 5–10 g of vegetable oil like corn oil, canola oil or peanut oil, the
mixtures are then centrifuged (1200–3000 g) for 10–25 min, the gain in volume per unit
weight is used as the measure of absorption.[76] Their studies also showed that the degree
of stabilisation has a profound effect on the absorption capacities of the extracted protein.
Patil & Khan,[84]’s studies suggest that Parboiling seems to aid oil absorption, contrary to
its effect on water absorption, the unfolding of protein structure and exposure of more
hydrophobic groups allows the physical entrapment of oil, making it clear that heat
treatment has a significant effect on absorption capabilities as it can directly affect the
protein’s structural conformation. Rice protein and its hydrolysates are seen to have lower
Oil absorption capacities as hydrolysis breaks protein chains, exposing internal hydro-
phobic groups. Good oil absorption properties of ingredients are critical to food systems
like sausages, nuggets and batters.[59,87] Rice bran proteins possess good oil absorption
characteristics with a value of 3.83 mL/g followed by Brown rice protein and White rice
protein with 2.93 mL/g and 2.56 mL/g, respectively.[76] RBP’s oil absorption values are
seen to be superior to both casein and soy protein isolates.[81]
Protein modification
As discussed in previous section, the rice protein has shown different functional properties
at different pH, salt & sugar concentration, etc., which are due to the structural and
conformational modification of protein caused by the external factors. The structure and
nature of protein plays a crucial role in deciding the protein functionality. During food
processing, various intrinsic and extrinsic factors of food results in modification in the
native structure and conformation of protein, thus leading to alteration in it is the way of
interacting with other food components. The changes occurred during processing may
have either desired or undesired effects on the functionality as well on the nutritive value
of proteins. For application in food model, one should have clear understanding of the
protein structure and its correlation with the specific functional property. The better
understanding of molecular basis for functional property of protein requires the compre-
hensive knowledge of the forces responsible for protein structure and its interaction.[88]
The structure – function relationship of protein largely depends on the covalent cross-
links naturally present. Altering the naturally present cross-links or introducing new
cross-links can result in the modification of the functional properties.[89] Various chemi-
cal, physical, and enzymatic methods have been employed for the protein modification
with the aim of enhancing nutritive values and functionality of protein. The chemical
modification involves the derivatization of few amino acids and side chains. Several
reactive side chains are present in the primary structure of protein and chemically
modifying them can result in functional enhancement of protein. Its aim is to change
the non-covalent forces responsible for protein conformation to obtain desired functional
enhancement.[90,91] Enzymes such as papain,[92] trypsin,[93] pronase,[94] etc., can also be
used for altering or extending the protein functionality. Enzymatic modification involves
the incorporation of inter-molecular or intra-molecular cross-links, or partial hydrolysis
of polypeptide chain, or introduction of specific group to the proteins.[91]
In recent studies various novel physical methods such as microfluidization,[74] high-
pressure processing,[95] freeze milling,[13] high-intensity ultrasound,[96] electron beam
irradiation,[97] radiofrequency,[98] extrusion cooking,[99] etc., have been explored for the
functional enhancement of proteins. Effect on the nutritive value and functionality of the
rice protein due to the different methods employed for protein modifications have been
studied by researcher. Few of the recent studies on rice protein modification using
different methods and their effect on protein functionality are depicted in Table 7. For
Table 7. Effect of various protein modification methods on the functionality of rice protein.
Protein
S. No. Modification method source Effect on functionality of protein References
[100]
1 Controlled enzymatic Rice Solubility and emulsification enhancement
hydrolysis endosperm
[97]
2 Electron beam Rice seed Improves solubility and emulsification
assisted enzymolysis
[101]
3 Glycosylation, Rice Enhancement of solubility and emulsifying properties
deamidation, endosperm
proteolysis
[13]
4 Freeze milling Rice seed Improved Foaming, emulsification and solubility
[102]
5 Glutaminase Rice seed Improved structural and sensory properties
treatment
[98]
6 Radio frequency Rice bran Improvement in absorption and emulsifying properties while
the negative effect on other functional properties
protein modification, the method needs to be selected carefully considering its final
application, effect on nutritive value, undesirable effect on the other functional properties,
toxic by-products which might develop during the processing or due to the reaction with
the other components of food, etc.
Applications of rice seed protein in food and allied industries

Rice bran proteins are an excellent source of nutrition and are generally considered
superior to the more conventional plant protein counterparts; it poses tremendous
potential to act as a novel food ingredient. They are known to exhibit various advanta-
geous functional properties that confer to it, the potential to be a low-cost high-quality
alternative to existing protein supplement options and find use in value-added
products.[103,104] The bran fraction of rice seed is the portion that contains most of the
protein inherent to the crop. Rice bran being a by-product of the commercial rice milling
industry continues to be largely under-utilized, its potential uses have been the subject of
research for decades but this has failed to extend to the industrial level. Most of the rice
bran discarded from milling industries is either used as alternative fuels for boilers and
heaters, as compacting/insulating material or as animal feed, thus the nutritional potential
of the material has largely been untapped. Various past studies have elucidated that
a majority of anti-nutritional factors in rice are proteinaceous in nature, excluding
phytates. Hence, alkali and acid treatments to remove them may pave the way for the
efficient usage and incorporation of rice proteins in food formulations.
The main hurdle in the incorporation of rice seed protein in various food-based
formulations lies in the efficient extraction of the protein fractions with minimal dete-
rioration and also achieving an appreciable level of solubility of the fractions in the desired
food systems, rice protein being poorly soluble in water has led to difficulties in its large-
scale incorporation. Concerns with regard to palatability are loss in flavour and darkened
colour, especially in the case of hydrolysed rice protein that possess a bitter taste.[105]
Pharmaceutical and therapeutic uses

Rice protein has shown very promising results in the various studies for its medicinal and
therapeutic uses. Rice protein and its hydrolysates can be used as bioactive compound
delivery system, as an effective natural antioxidant, exhibits antitumor properties, and is

effective for the treatment of hypertension. Rice is one amongst the principle foods that an
infant is introduced to post the weaning period. Hydrolysed formulas based on rice
protein have been considered in the treatment of cow’s milk protein allergy (CMPA) in
infants. Rice protein formulas supplemented with lysine and threonine have been shown
to mimic the amino acid profile of breast milk and thus can act as a potential alternative
food. Recent studies have shown that children with CMP allergy also tend to show adverse
reactions to casein and soy-based derivatives, thus paving the way for rice protein-based
products.[15,106]
The RPI-based diet can be an effective way to prevent the risk of cardiovascular disease.
The onset of cardiovascular disease is due to an inflammatory process known as athero-
sclerosis. Study on apolipoprotein E knockout mice fed with rice protein isolate diet by
Burris et al.[107] has reported the anti-atherosclerotic effect of rice protein. In their study, it
was observed that rice protein isolate fed diet helped in the reduction in the atherosclero-
tic streak lesion formation.
Rice seed protein fractions are known to be good inhibitors of the angiotensin-
converting enzyme, thus aiding in the relief of hypertension and can be utilized as
a potential pharmaceutical component to counter cardiovascular ailments.[16] Rice Bran
Protein isolates have been attributed to disease control and seen to possess anticancer
properties.[104]
A lipoprotein fraction isolated from RBPs exhibited some antitumor properties, the
protein fraction was observed to inhibit the development and proliferation of cultured
human endometrial adenocarcinoma cells.[108] Detailed and rigorous study on this topic
has however been limited. Rice bran being a good source of important micronutrients and
minerals such as iron, zinc, manganese, calcium and magnesium reinforces its potential
for usage in food fortification and incorporation as a value-adding ingredient.
Meat products
The various functional and nutritional advantages possessed by rice protein have paved its
way for the application in food formulation and food processing. The strong antioxidant
property of rice protein hydrolysates (RPH) is effective in improving the shelflife of the
meat products by preventing the lipid oxidation. Zhou et al.[109] studied the effect of
addition of RPH on the lipid peroxidation in the cooked ground beef and reported that
RPH can be used in food models to inhibit the lipid oxidation.
In another study, it is reported that fortification of beef patties with rice protein has not
only increased protein content but also reduces cooking loss, and improved the redness
value which is desirable according to consumer point of view. Also, rice protein is found
to show better antioxidant properties in comparison to pea protein isolate and lentil
flour.[110] Rice protein is a natural antioxidant and can be used to replace the artificial
antioxidants.
Baking
Stabilized or parboiled rice bran has appealing characteristics to be used in food formula-
tion. For example, the granulated powder of bran having a cream colour with tasteless and
odourless properties may be useful as a thickening, bulking, or flavouring agent in product

formation. It is mostly used in bakery products, possibly because of functional properties
of the proteins, which may improve rheological behaviour of the dough as desired in the
end-use quality.[111] Studies incorporating acid-stabilized rice bran (ASRB) and heat
stabilized rice bran (HSRB) in baked products like cookies have shown to increase the
nutritional quality of the product in terms of overall protein, mineral content and
moisture carrying capacity, it is also seen to have a minimising effect on the baking spread
of cookies which consequently results in slightly thicker products.[112] Cookies substituted
with HSRB were shown to consistently outperform ASRB substituted cookies in sensory
evaluation but both scored lower than non-substituted cookies, the most acceptable
substitution ratio was seen to be 75:15 (wheat flour: rice bran). Moreover, cookies
supplemented with rice bran exhibited a significant increase in mineral content.
Edible films, coating and encapsulation

The possibility of utilizing rice seed protein to create sturdy edible films has been a topic
of interest for many years; the main objective has been to arrive at a film that possesses
appreciable tensile strength and other physical properties. Edible films may also act
carriers for nutrients, flavours, antioxidants and other preservatives that can further
enhance shelf life and add value to the product. Moreover, the use of edible films may
help in reducing the reliance on plastic for most food packaging purposes, thus reducing
the damage on the environment as a whole. Rice is a staple food for nearly 50% of our
world’s population,[113] thus efficient usage of rice milling by-products and their value
addition is an exciting and critical venture.
Protein-based films are generally stronger than lipid-based films and tend to be
excellent oxygen barriers due to their tightly packed, ordered hydrogen-bonded network
structure. Protein films are formed by the extended polypeptide structures that are formed
on denaturation by acid, alkali or other treatments, these structures associate through
hydrogen, ionic, hydrophobic and covalent bonding to form the protein matrix.[114] Low
molecular weight plasticizers such as glycerol, sorbitol and lipids are incorporated to
improve flexibility by reducing the chain-to-chain interactions.[115] The film formation
mechanism then proceeds via protein polymerisation and solvent evaporation at the
interface between film and air. Protein molecules in the film associate through disulphide,
hydrophobic, hydrogen bonds.[116]
Edible films prepared using 53% rice protein concentrate and pullulan as the principal
components along with propyleneglycol alginate (PGA) have yielded films with appreciable
properties, PGA aids in the cross-link formation between protein peptides greatly influences the
setting of the protein-polysaccharide film. Pullulan is a polysaccharide produced by
Aureobasidium pullulans from sugars, it aids in improving the mechanical properties of the
film such as tensile strength and water vapour permeability. Films made from protein solution
(5% w/v) at different pH and concentration of glycerol (plasticizer) were prepared and analysed
by Shih,[117] and it was found that puncture strength was influenced by the purity of the protein,
its composition and structure. Lower concentration of glycerol (2% w/v) resulted in films with
better puncture strength and water solubility. Alkaline conditions (8.0pH) were also seen to
produce relatively strong films. Factorial experiment designs were used to evaluate the effect of
adding protein, montmorillonite (MMT) clay, phenolic extract, glycerol concentrations on film
properties.[17] The best properties were obtained for rice bran protein films with lower protein
and glycerol concentrations and with the addition of phenolic extract without the presence of
MMT clay. Solubility was mainly influenced by protein concentration, parameters such as
luminosity and opacity of the films also followed a similar trend. However, in case of mechanical
properties, glycerol concentration was the main factor. Phenolic extract addition affected film
opacity, tensile strength and elongation. The major challenge associated with protein or poly-
saccharide films is that they have brittle structure at low relative humidity or low strength at high
relative humidity; thus, modification of film strength and water sensitivity is generally achieved
by changing processing procedures and varying the composition of the mixture by adding
components that strengthen and promote film setting.[118] Studies employing starch and protein
from broken rice to make edible films with appreciable characteristics were also carried out by
Dias et al.[119] They were able to arrive upon films whose properties were similar to solely starch-
based films but possessing remarkably higher vapour permeability. It is also noted that addition
of sorbitol yields better mechanical rigidity and lowers water permeability, but glycerol addition
confers the opposite effect.
Protein-based coating is an alternative way of extending the shelf life of food products.
The rice protein possesses excellent barrier properties and can be used as edible coating
material. Using rice protein extracted from the by-products of rice milling for food
coating may provide us an economical and sustainable solution. da Silva et al.[120] have
reported that rice protein-based coating with suitable plasticizer can be used to preserve
the internal quality and extending the shelf life of eggs. The rice protein-based coating
blocks the pores of shell surface thus resulting in preserving the quality of albumen and
yolk. The use of sorbitol as plasticizer instead of glycerol and propylene glycol is efficient
in maintaining and controlling the increase in the pH of albumen.
Proteins and various polysaccharides have been studied for the encapsulations of bioactives
such as drugs, carotenoids, polyphenols, vitamins, etc. Encapsulation has numerous advan-
tages such as decrease core material reactivity; prevent core material from physical and
chemical damage during processes, controlled release of drugs and bioactive compounds,
etc. Wang et al.,[13] in their study fabricated oil droplets having modified rice protein shell and
core of soybean oil core and studied its potential application for oral delivery of lipophilic
bioactive. The rice protein has extra advantageous compared to soy and dairy protein because
of its hypoallergenicity and other health benefits. The β-carotene encapsulated in these oil
droplets having modified rice protein shell enabled the partial release of β-carotene during the
simulated gastric digestion, while during the succeeding stimulated intestinal digestion
encapsulation enabled the controllable zero-order release rate of β-carotene.
Conclusion
Rice seed protein holds immense potential to act as a healthy, economic and widely
available protein source for consumption; it can act as an excellent novel ingredient and
a quality alternative for existing cereal and animal-based protein options. Its excellent
nutritional content and functional properties make it a highly utilisable option in various
food formulations. Rice seed protein is of excellent quality, possessing appreciable biolo-
gical value, digestibility and efficiency ratios that are comparable to and even exceed those
of casein and soy protein. They also have a sound amino acid profile comprising of
essential amino acids such as threonine, leucine and phenylalanine along with sulphur-
rich amino acids like methionine and cysteine which are critical for the human body. Rice
seed protein’s hypoallergenicity is a unique trait that enables its incorporation in infant
food formulations and supplements for treating ailments like Cow Milk Protein allergy
and cardiovascular relief. It is also seen to possess bioactive compounds that aid in body
regulation and gut relaxation along with excellent antioxidative properties. Studies have
also highlighted that rice protein derived films can act as sufficiently strong edible
packaging with good barrier properties; it can also act as filler material in meat products.
Moreover, the usage of rice protein extracted from the milling by-products of paddy
would significantly reduce the environmental load caused by them and effectively increase
the value of these underutilised products that are either burnt, used as fodder or fuel. The
main hurdles in the commercialisation of rice protein are the difficulty in efficiently
extracting the protein fractions without causing excessive modification at large scales
and the time required to achieve extraction. Moreover, its lower overall protein content
and the internal distribution of protein fractions make it difficult to find a suitable
solubilising solvent for extraction and its incorporation in food.
Acknowledgments
The support from Department of Food Science and Technology, NIFTEM and NIFTEM Knowledge
Centre is greatly acknowledged.
Disclosure statement
Author and co-authors declare no conflict of interest.
ORCID
Neeraj Ghanghas http://orcid.org/0000-0002-0683-2065
Pramod K. Prabhakar http://orcid.org/0000-0002-1967-6575
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ISSN: 8755-9129 (Print) 1525-6103 (Online) Journal homepage: https://www.tandfonline.com/loi/lfri20

Classification, Composition, Extraction, Functional

Neeraj Ghanghas, Mukilan M. T., Shikha Sharma & Pramod K. Prabhakar

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Classiﬁcation, Composition, Extraction, Functional

Rice grain: structure and milling

Rice seed composition

Rice seed protein

Rice seed protein classiﬁcation

Table 4. Protein content of rice bran reported in past studies.

fractions compared to other proteins. Prolamins constitute 2.6–3.3% & about 4% of

Amino acid composition

Rice protein extraction methods

Table 5. Amino acid composition of various protein sources.

Table 6. Amino acid composition of various rice cultivars.

Ultrasonic assisted alkali extraction

Extraction by fractionation method

Enzymatic extraction method

Functional properties of rice seed protein

hydrophobicity of protein results in the decrease in emulsifying properties of protein as it

Oil absorption capacity

Applications of rice seed protein in food and allied industries

Pharmaceutical and therapeutic uses

delivery system, as an eﬀective natural antioxidant, exhibits antitumor properties, and is

odourless properties may be useful as a thickening, bulking, or ﬂavouring agent in product

Edible ﬁlms, coating and encapsulation

[45] Kaewka, K.; Therakulkait, C.; Cadwallader, K. R. Eﬀect of Preparation Conditions on

[83] Pearce, K. N.; Kinsella, J. E. Emulsifying Properties of Proteins: Evaluation of

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