Documenti di Didattica
Documenti di Professioni
Documenti di Cultura
Review
a r t i c l e i n f o a b s t r a c t
Article history: Background: Rice is a staple food and an important source of proteins in many regions worldwide. Its
Received 22 February 2016 protein component is generally regarded as hypoallergenic, and a number of studies have highlighted the
Received in revised form nutritional and health benefits associated with consumption of rice proteins. In recent years, the pro-
20 January 2017
cessing of plant proteins has drawn scientific and industrial interest, and rice protein-enriched in-
Accepted 30 January 2017
Available online 27 February 2017
gredients have become commercially available.
Scope and Approach: The aim of this study was to provide a critical review of the state of the art
regarding the composition, extraction methods, functional properties and applications of rice proteins.
Keywords:
Rice proteins
Key Findings and Conclusions: Rice is composed of four protein fractions, namely albumin (water-solu-
Composition ble), globulin (salt-soluble), glutelin (alkali-soluble), which represents the dominant protein in brown
Rice protein fractions and milled rice, and prolamin (alcohol-soluble), a minor protein in all rice milling fractions. Different
Extraction methods methods to extract proteins from rice, including alkaline, enzymatic and physical methods, have been,
Functional properties and continue to be, evaluated for their efficacy, and some have been applied industrially. However, only a
Applications limited amount of studies have described the functional properties of rice proteins and how these can be
improved by means of enzymatic hydrolysis. Applications of intact rice proteins are limited due to their
poor solubility in water. However, hydrolysed rice proteins are used in the formulation of hypoallergenic
infant formulas and may potentially be used in a variety of food systems due to their improved func-
tionality. Despite the advances in the characterisation of rice proteins, a greater understanding of their
physicochemical properties and how to modify their functionality is required in order to expand their
range of food applications.
© 2017 Elsevier Ltd. All rights reserved.
http://dx.doi.org/10.1016/j.tifs.2017.01.008
0924-2244/© 2017 Elsevier Ltd. All rights reserved.
2 L. Amagliani et al. / Trends in Food Science & Technology 64 (2017) 1e12
2007; Kannan, Hettiarachchy, & Mahedevan, 2012; Zhang, Bartley, protein fraction in brown and milled rice, whereas prolamin, which
Mitchell, Zhang, & Yokoyama, 2011) activities. Therefore, rice rep- represents the major endosperm storage protein in all other cereals
resents an interesting source of proteins for the development of except oats (Shewry & Halford, 2002), is a minor protein in all rice
protein-enriched ingredients for the formulation and manufacture grain milling fractions.
of nutritional products. Differences in protein composition of the rice milling fractions
result in differences in the nutritional quality of their protein
2. Distribution and composition of proteins in rice component. Han, Chee, and Cho (2015) showed that rice bran
protein has a higher nutritional quality than rice endosperm pro-
The protein content of rice is usually calculated from Kjeldahl tein; protein efficiency ratio (PER), net protein retention (NPR) and
nitrogen multiplied by the nitrogen-to-protein conversion factor of net protein utilisation (NPU) were 2.39, 3.77 and 70.7, respectively,
5.95, which is based on the nitrogen content (16.8%) of glutelin, the for rice bran protein, and 1.96, 3.26 and 61.4, respectively, for rice
major rice protein, although a nitrogen-to-protein conversion fac- endosperm protein. PER and NPR were higher for both rice protein
tor of 6.25 is used in nutritional studies in order to maintain a ingredients compared to soy protein isolate (SPI) (1.71 and 3.04,
common nitrogen-based calculation for all proteins (Shih, 2004). respectively, for SPI), but lower compared to casein (2.58 and 4.02,
Rice grain milling fractions differ in terms of protein content, with respectively, for casein) and whey protein isolate (WPI) (3.26 and
that of brown rice, i.e., the rice caryopsis, being higher compared to 4.54, respectively, for WPI). Of those protein ingredients analysed
milled or white rice (composed entirely of endosperm) due to the by Han et al. (2015), WPI was the only ingredient with a higher NPU
removal of the protein-rich bran during milling (Table 1). Rice bran (74.0) than rice bran protein. Also, rice bran protein had true di-
consists of a fine, floury material, which includes pericarp, seed gestibility (TD), biological value (BV) and protein digestibility-
coat, nucellus, aleurone, pulverized embryo, and some hull and corrected amino acid score (PDCAAS) of 94.8%, 72.6% and 0.90,
endosperm fragments (Orthoefer & Eastman, 2004) (Fig. 1). The respectively, whereas the same indices for rice endosperm protein
protein content of rice is influenced by factors such as management were 90.8%, 66.7% and 0.63, respectively. PDCAAS of rice endo-
and cultural practices, climate and genotype (Champagne, Wood, sperm protein, but not that of rice bran protein, was considerably
Juliano, & Bechtel, 2004). lower compared to that of the other ingredients analysed, which
had values ranging from 0.95 (SPI) to 1.00 (casein and WPI).
However, for both rice protein ingredients, TD was comparable to
2.1. Rice protein fractions
that of SPI (91.7%) and dairy protein ingredients (92.8e94.8%),
whereas BV was lower than only that of WPI (78.8%). Furthermore,
Rice proteins are categorized according to the solubility-based
rice endosperm and rice bran proteins had a similar content of total
classification described by Osborne (1924); albumin (water-solu-
essential amino acids (41.1e41.7 g/100 g protein) to that of SPI
ble), globulin (salt-soluble), glutelin (alkali/acid-soluble), and pro-
(41.2 g/100 g protein), but these values were significantly lower
lamin (alcohol-soluble) are the four main rice protein fractions.
compared to those observed for casein and WPI (50.6e55.2 g/100 g
Rice proteins are mainly observed in the form of storage or-
protein) (Table 3).
ganelles called protein bodies (PBs). Two types of morphologically
An analysis of the amino acid profile of individual rice proteins
distinct PBs have been identified in rice endosperm, namely type I
(Table 4) shows that prolamin has the lowest content of lysine, the
(PB-I) and type II (PB-II) (Fig. 2). PB-I has a lamellar structure, is
first limiting amino acid among cereal proteins (Young & Pellett,
spherical in shape and is rich in prolamin, whereas PB-II has a
1994). The highest lysine content is found in albumin, followed
crystalline structure, displays an irregular shape and contains
by glutelin and globulin. Being rich in albumin, rice bran displays a
predominantly glutelin (Bechtel & Juliano, 1980; Bechtel &
higher content of lysine compared to brown or milled rice. Also, due
Pomeranz, 1978; Ogawa et al., 1989, 1987; Tanaka, Sugimoto,
to the low content of prolamin, rice has a higher lysine content than
Ogawa, & Kasai, 1980). According to Ogawa et al. (1987), endo-
other cereal grains (Day, 2013). As regards the other essential amino
sperm storage proteins comprise 60e65% PB-II, 20e25% PB-I and
acids, albumin shows the highest content of histidine and threo-
10e15% albumin and globulin in the cytoplasm.
nine, whereas prolamin has the highest proportions of isoleucine,
Rice grain milling fractions differ in terms of protein composi-
leucine and phenylalanine. Furthermore, globulin has the highest
tion (Table 2). Data reported in the literature regarding rice protein
content of the sulfur-containing amino acids cysteine and methi-
solubility fractions vary widely, depending on the rice variety and
onine, while prolamin has the lowest. Based on their amino acid
the extraction procedures. Albumin, globulin, glutelin and prolamin
composition, albumin has been estimated to have the highest and
have been reported to account for 5e10, 7e17, 75e81 and 3e6%,
prolamin the lowest BV among the rice protein fractions (Padhye &
respectively, of total protein in brown rice, 4e6, 6e13, 79e83 and
Salunkhe, 1979).
2e7%, respectively, of total protein in milled rice, and 24e43,
13e36, 22e45 and 1e5%, respectively, of total protein in rice bran
2.1.1. Albumin
(Adebiyi, Adebiyi, Hasegawa, Ogawa, & Muramoto, 2009a; Agboola,
Albumin is readily soluble in water due to the presence of suf-
Ng, & Mills, 2005; Cao, Wen, Li, & Gu, 2009; Ju, Hettiarachchy, &
ficient net charge and the lack of any extensive disulfide cross-
Rath, 2001; Juliano, 1985; Zhao et al., 2012a). Glutelin is the main
linking or aggregation (Hamada, 1997). However, globulin
contamination occurs when albumin is extracted with water,
Table 1 because of minerals present in the rice grain that dissolve in water,
Chemical composition (%) of rice grain milling fractions at 14% moisture (adapted thus increasing the solubility of globulin (Villareal & Juliano, 1981).
from Juliano & Bechtel, 1985). Therefore, in order to obtain purified albumin at laboratory scale,
Brown Milled Bran additional steps have to be carried out, which include repeated
precipitation, centrifugation and dialysis (Hamada, 1997; Iwasaki,
Protein (N 5.95) 7.1e8.3 6.3e7.1 11e15
Crude fat 1.6e2.8 0.3e0.5 15e20 Shibuya, Suzuki, & Chikubu, 1982; Mawal, Mawal, & Ranjekar,
Available carbohydrates 73e76 77e78 34e52 1987). Application of isoelectric focusing (IEF) (pH 3.5e10) to mil-
Starch 66 78 14 led rice albumin revealed 16e18 bands, 10e11 of which had iso-
Crude fiber 0.6e1.0 0.2e0.5 7.0e11 electric point (pI) in the range 6.0e7.5 (Villareal & Juliano, 1981).
Crude ash 1.0e1.5 0.3e0.8 6.6e9.9
However, only one band, with pI 6.4, was found in the study of
L. Amagliani et al. / Trends in Food Science & Technology 64 (2017) 1e12 3
Fig. 2. Schematic structure of rice protein bodies and compound starch granule in the endosperm subaleurone layer (from Coffman & Juliano, 1987).
Table 2 Padhye and Salunkhe (1979), whereas Mawal et al. (1987) reported
Distribution (%) of rice proteins among rice grain milling fractions (data collated a major fraction of rice albumin to be a 60 kDa glycoprotein with pI
from Adebiyi et al., 2009a; Agboola et al., 2005; Cao et al., 2009; Ju et al., 2001;
6.5. Following extraction from defatted rice flour, turbidity mea-
Juliano, 1985; Zhao et al., 2012a).
surement of the supernatant indicated that albumin had pI of pH
Brown Milled Bran 4.1 (Ju et al., 2001).
Albumin 5e10 4e6 24e43 Gel filtration on Sephadex G-100 showed the molecular weight
Globulin 7e17 6e13 13e36 (MW) of milled rice albumin to range from 10 to 200 kDa (Iwasaki
Glutelin 75e81 79e83 22e45
et al., 1982). According to Hamada (1997), fully dissociated rice bran
Prolamin 3e6 2e7 1e5
4 L. Amagliani et al. / Trends in Food Science & Technology 64 (2017) 1e12
Table 3 10e150 kDa (Hamada, 1997). Brown rice globulin was resolved by
Essential amino acid (EAA) composition (g/100 g protein) of rice endosperm protein SDS-CE into 6 subunits with MW ranging from 23 to 105 kDa, with
(REP), rice bran protein (RBP), soy protein isolate (SPI), casein and whey protein
isolate (WPI) (adapted from Han et al., 2015).
the 54 kDa one being predominant (Agboola et al., 2005).
its low starch content, and has mainly been used as an ingredient in with thermal stabilisation reducing the extractability of proteins
animal feed or even as boiler fuel (Fabian & Ju, 2011; Shih, 2003). and altering the protein profile and amino acid composition of the
However, the nutritional and health properties of plant proteins in extracted proteins (Gnanasambandam & Hettiarachchy, 1995; Khan
general, and rice proteins in particular, are widely recognized today, et al., 2011; Prakash & Ramanatham, 1994).
and rice protein-containing products have become commercially In vitro and in vivo studies demonstrated that rice proteins
available in recent years. The increasing interest of industry and the prepared by alkaline extraction have higher digestibility and
academic research communities in these ingredients enabled the bioavailability compared to those prepared by degradation of starch
development of processes for the extraction, enrichment, purifi- by a-amylase as a result of the structural changes in the poorly
cation and functionalisation of rice proteins. Alkaline, enzymatic digestible PB-I caused by alkaline extraction (Kubota et al., 2010;
and physical treatments have all been, and continue to be, evalu- Kumagai et al., 2006, 2009). However, alkaline extraction pre-
ated for their potential in the extraction of proteins from rice, and sents some drawbacks, as alkaline conditions could lead to (i)
some have been applied industrially. denaturation and hydrolysis of proteins, (ii) increased extraction of
The processing of rice bran proteins represents a challenge. Rice non-protein components that co-precipitate with proteins,
bran contains high amounts of fat, i.e., 15e20% by weight (Table 1), lowering the protein purity of the resultant ingredient, (iii)
which provides a substrate for the activity of lipase, lipoxygenase increased Maillard reactions (due to high pH) resulting in dark
and peroxidase enzymes, resulting in the development of rancidity coloured (i.e., melanoidin-based) products, and (iv) the formation
and off-flavours (Orthoefer & Eastman, 2004). Therefore, rice bran of toxic compounds such as lysinoalanine (Otterburn, 1989; Wang,
needs to be defatted (by hexane extraction, wet extrusion or me- Hettiarachchy, Qi, Burks, & Siebenmorgen, 1999).
chanical pressing) or stabilised by heat treatment (e.g., retorting,
extrusion cooking, fluidized bed drying, microwave heating, ohmic 3.2. Enzymatic extraction
heating, pan roasting or parboiling) or reduction of pH in order to
inhibit lipase and oxidative enzymes (Khan et al., 2011; Lakkakula, Extraction of proteins from rice flour and rice bran for food
Lima, & Walker, 2004; Orthoefer & Eastman, 2004; Ramezanzadeh, applications is normally achieved by means of enzymatic methods.
Rao, Prinyawiwatkul, Marshall, & Windhauser, 2000; Sayre, Depending on rice cultivar, degree of milling and enzymatic treat-
Saunders, Enochian, Schultz, & Beagle, 1982). However, several of ment, products with protein content higher than 90% (i.e., protein
these treatments have the potential to induce protein denaturation isolates) can be obtained by the processing of rice flour with starch-
and/or aggregation, thus reducing protein solubility and making hydrolysing enzymes. Since starch represents the major constituent
the processing of rice bran proteins even more challenging. of rice endosperm, enzymes such as a-amylase, glucoamylase and
Furthermore, rice bran contains fiber (7e11%) and phytate pullulanase, which solubilise starch, are often used to separate
(0.9e2.2%) (Orthoefer & Eastman, 2004), which are extensively proteins in rice flour (Shih, 2003). However, because of the high
associated with/bound to proteins, making the separation of pro- cost and low protein content of milled rice and rice flour, rice
tein bodies from these components difficult to achieve (Tang, proteins can be more conveniently extracted from a low-cost
Hettiarachchy, & Shellhammer, 2002). On the other hand, rice source such as rice dregs, a by-product from the processing of
flour contains endosperm storage proteins, which appear to be rice syrups, which has protein content higher than 50% (Zhao et al.,
more readily extractable than rice bran proteins (Shih, 2003). 2013). In the study of Shih and Daigle (2000), treatment of a
protein-enriched rice flour (brown rice protein concentrate) with
3.1. Alkaline extraction Termamyl 120L (an a-amylase) (at pH 6.5, 90 C) followed by Dia-
zyme L200 (a glucoamylase; at pH 4, 60e62 C), resulted in a
In the food industry, alkaline treatment of rice flour is generally product (insoluble fraction) with 85% protein, which was increased
applied to facilitate removal of the endosperm proteins for the to 91% protein by a subsequent treatment with Viscozyme L (a
production of purified starch, as opposed to direct extraction of multi-enzyme complex containing a range of carbohydrate-
proteins, with the protein fraction being traditionally discarded or digesting enzymes, including arabanase, cellulase, b-glucanase,
used as an ingredient in animal feed formulations (Shih, 2003). hemicellulase and xylanase).
However, alkaline conditions are particularly effective in extracting Carbohydrate-digesting enzymes (e.g., cellulase, hemicellulase,
proteins from rice flour, where glutelin is the dominant protein pectinase and xylanase), which hydrolyse high MW cell wall
fraction. Cagampang, Cruz, Espiritu, Santiago, and Juliano (1966) components, have mainly been employed to enhance protein
reported that dilute alkaline solvents (e.g., 0.1 N potassium or so- extractability from rice bran, by liberating proteins from the
dium hydroxide) extracted up to 97% of total proteins from milled polysaccharide-based structures. Ansharullah, Hourigan, and
rice flour. According to Paraman, Hettiarachchy, and Schaefer Chesterman (1997) reported that treatment of full-fat extruded
(2008), alkaline extraction (pH 11, 40 C) of milled rice flour fol- rice bran with Viscozyme L at pH 3.8 and 50 C would result in the
lowed by either ultrafiltration or isoelectric precipitation of the extraction of 58% nitrogen, as predicted by response surface
supernatant provided products with 71 and 86% protein, respec- methodology. A rice bran protein isolate with a protein content of
tively, with proteins recovered by ultrafiltration having superior 92% and a protein yield of 75% was prepared from defatted unsta-
functional properties. bilised rice bran using a combination of phytase and xylanase (pH 5,
Alkaline treatment followed by isoelectric precipitation (pH 55 C) (Wang et al., 1999); however, the alkaline treatment applied
4e4.5) has also been used for the extraction of proteins from rice (pH 10) to inactivate the enzymes prior to the recovery of proteins
bran, resulting in products with protein contents ranging from may have caused an increase in protein extractability. Using the
about 40 to >80% (Bandyopadhyay, Misra, & Ghosh, 2008; Chandi & same combination of enzymes and a similar extraction method as
Sogi, 2007; Gnanasambandam & Hettiarachchy, 1995; Wang et al. (1999), Khan et al. (2011) obtained protein concentrates
Jiamyangyuen, Srijesdaruk, & Harper, 2005; Prakash & from defatted unstabilised and heat-stabilised (microwave, dry
Ramanatham, 1994; Yadav, Yadav, & Chaudhary, 2011). Rice heat, parboiling) rice bran having protein contents ranging from
cultivar, degree of milling, specific alkaline conditions, the use of 61% (parboiled rice bran) to 85% (unstabilised rice bran).
unstabilised or stabilised rice bran, and the stabilisation technique Proteases have also been used for extracting proteins from rice;
employed may account for differences in terms of protein content, a number of food-grade commercially available proteases of animal,
6 L. Amagliani et al. / Trends in Food Science & Technology 64 (2017) 1e12
bacterial, fungal or plant origin have been evaluated for this pur- An emerging method for the extraction of proteins from rice is
pose. However, the protein extracted with the aid of protease that based on the use of water at subcritical conditions. Subcritical
treatment is hydrolysed (i.e., the product is a hydrolysate), with water (SW) extraction employs water at temperatures between 100
different structural and physicochemical properties to the intact and 374 C (the latter being the critical temperature of water) and
proteins. Treatment of broken rice flour with an alkaline protease pressure high enough to maintain its liquid state. When the tem-
(pH 10, 45 C) or papain (pH 7, 50 C) generated protein hydroly- perature of the water is increased from ambient to 250 C, its
sates with protein contents (calculated from nitrogen levels, and relative dielectric constant decreases from around 80 to values
thus including intact proteins and fragments thereof) of 56 and close to 27, which is similar to that of ethanol at ambient temper-
65%, respectively, with protein recoveries being 75 and 46%, ature (Herrero, Cifuentes, & Iban ~ ez, 2006); therefore, SW has the
respectively (Hou, Zhu, & Li, 2010). In the study of Li et al. (2012), a ability to dissolve hydrophobic material. Also, because at subcritical
hydrolysate with a protein content of 81%, protein recovery of 76%, conditions the dissociation constant of water (Kw) to hydrogen and
and degree of hydrolysis (DH) of 7% was obtained by treating rice hydroxyl ions is much greater than that of ambient water, SW can
dregs with trypsin under optimised conditions (pH 7.6, 52.8 C). catalyse chemical reactions such as degradation and hydrolysis
Nitrogen yields of rice dregs-based protein hydrolysates generated (Hata, Wiboonsirikul, Maeda, Kimura, & Adachi, 2008;
using Neutrase (pH 7.6, 50.4 C), Alcalase (pH 9.2, 50.2 C), Wiboonsirikul et al., 2007); therefore, biomolecules such as car-
bromelain (pH 7.3, 56.5 C) or papain (pH 6.9, 51.5 C) under bohydrates (Haghighat Khajavi, Ota, Kimura, & Adachi, 2006) and
optimal conditions were 49, 57, 31 and 17%, respectively, with the proteins (Sereewatthanawut et al., 2008; Sunphorka, Chavasiri,
protein contents of the products being 79, 63, 58 and 55%, Oshima, & Ngamprasertsith, 2012; Watchararuji, Goto, Sasaki, &
respectively (Guo, Zhang, Ma, & Tian, 2013). Shotipruk, 2008) can be hydrolysed in SW without any additional
Hamada (1999) reported that about 74e92% of the proteins of catalyst.
defatted rice bran could be extracted by treatment with Opticlean SW has been utilised to extract various functional compounds
(an alkaline protease) (pH 8 or 10, 40 C) to 2e10% DH values. (proteins, amino acids, carbohydrates and phenolics) from rice bran
Alcalase and Flavourzyme (pH 8, 50 C), extracted 81 and 88% of (Hata et al., 2008; Sereewatthanawut et al., 2008; Watchararuji
proteins from defatted rice bran, respectively, resulting in protein et al., 2008; Wiboonsirikul et al., 2007). Treatment of rice bran
hydrolysates having protein contents of 28% (DH 7.5%) and 30% (DH with water at subcritical conditions has provided high protein
8.8%), respectively (Hamada, 2000). yields. In the study of Watchararuji et al. (2008), 84% of protein was
extracted from defatted rice bran using SW at 220 C for 30 min.
3.3. Physical extraction Sereewatthanawut et al. (2008) reported that the amount of pro-
tein recovered from defatted rice bran in the extract solubilised by
Physical methods are usually preferred to chemical or enzymatic SW treatment at 200 C for 30 min was comparable to the amount
methods in the processing of food, as they induce less modifica- in the original bran. This was mainly attributed to the breakdown of
tions (Shih, 2003), as well as generally being more economical and proteins into soluble peptides or amino acids, due to the increase of
easier to be adapted and utilised in industry. Freeze-thaw, high- Kw at high temperatures. Sunphorka et al. (2012) proposed a
speed blending, sonication, hydrothermal cooking (HTC), micro- mechanism to explain the changes occurring in rice bran proteins
fluidization and the use of subcritical water (SW) are among the during SW treatment, which includes three steps: (i) protein ag-
physical approaches tested to extract proteins from rice. gregation, (ii) protein disaggregation by hydrolysis to polypeptides
Several physical treatments (i.e., freeze-thaw, high-speed and (iii) amino acid liberation; these steps follow first-, second- and
blending, high pressure and sonication) have been investigated for zero-order reaction kinetics, respectively. Soluble rice bran extracts
their effectiveness in facilitating the extraction of proteins from resulting from SW extraction displayed radical scavenging and
heat-stabilised defatted rice bran (Tang et al., 2002). Among the antioxidant activity (Hata et al., 2008; Sereewatthanawut et al.,
physical treatments tested, sonication gave the highest protein 2008; Watchararuji et al., 2008; Wiboonsirikul et al., 2007;
extraction yield, but this was only 15%. However, protein extract- Wiboonsirikul, Kimura, Kanaya, Tsuno, & Adachi, 2008). Although
ability increased significantly when these physical treatments were SW treatment appears to be a promising technique for the
coupled with the action of enzymes such as a-amylase and Protease extraction of proteins from rice, so far it has only been used as a
P. According to Xia et al. (2012a), colloid milling of broken rice batch process at pre-commercial scale and further research is
followed by microfluidization and density-based separation pro- required to evaluate the quality, stability and functionality of the
vided protein yield of 82% and protein purity of 44%, with protein extracted proteins.
purity increasing further to 88% when subsequently treated with
amylase and glucoamylase enzymes. The proteins obtained using
this method had higher in vitro digestibility but considerably lower 4. Functional properties of rice proteins
solubility in the pH range 6e10 than those obtained by alkaline
extraction. Xia et al. (2012b) employed HTC, a steam-infusion The utilisation of proteins as food ingredients depends on their
treatment characterised by high temperature and shearing, to functional properties. These properties, which determine the
extract proteins from heat-stabilised rice bran. Protein yield and behaviour and performance of proteins in food systems (i.e., func-
protein purity were 37 and 28%, respectively, at 120 C, and 50% and tionality) during preparation, processing, storage and consumption,
53%, respectively, at 150 C. When combining HTC processing with are influenced by the nature and extent of interactions of the
amylase pre-treatment at 120 C or 150 C, protein purity levels proteins with themselves, with other components, and with water
increased from 28-53% to 72e74%, whereas protein yield improved in the food system (Panyam & Kilara, 1996). The functional prop-
only for the 120 C treatment (from 37 to 45%). In contrast, alkaline erties required depend on the application of the protein in-
extraction followed by acid precipitation resulted in lower protein gredients. Since many formulated foods are physically presented as
yield (15%) at a protein purity of 68%. Depending on HTC temper- beverages, emulsions or foams, the protein ingredients used in
ature and amylase pre-treatment, HTC-prepared protein isolates their formulation have to possess good solubility, heat stability and
exhibited higher surface hydrophobicity, sulfhydryl and disulfide surface-active properties. Water and oil absorption ability of pro-
bond contents, and superior emulsifying properties, compared to teins are also essential properties for the formulation of a range of
alkali-extracted proteins. processed foods.
L. Amagliani et al. / Trends in Food Science & Technology 64 (2017) 1e12 7
96e98%, and about 90% being soluble at pH 5. Conversely, alkali- In addition to the applications of isolated rice protein in-
extracted rice dregs proteins had solubilities of 62% at pH 7 and gredients, it is worth mentioning that rice flour currently repre-
only 8% at pH 5. Also, EA and ES of the hydrolysates at pH 7 were in sents the most commonly used ingredient in the production of
the range 30e45% and 11e17%, respectively, whereas those of gluten-free products on the market, such as bread and pasta,
alkali-extracted proteins were 17 and 12%, respectively. Functional with rice proteins contributing significantly to the quality and
properties of a defatted rice bran protein isolate (alkali-extracted) technological functionality of these products (Hager, Wolter, Jacob,
improved upon papain treatment (pH 8, 50 C) for 10e60 min Zannini, & Arendt, 2012; Moroni, Iametti, Bonomi, Arendt, & Dal
(Bandyopadhyay et al., 2008). Solubility of the protein isolate was Bello, 2010). Despite the technological difficulties related to the
29, 54, 80 and 85% at pH 3, 5, 7 and 9, respectively, whereas solu- use of gluten-free flours in bread-making, due to the fact that, after
bility of the hydrolysates at the same pH values was in the range hydration and mixing, proteins do not develop into a viscoelastic
30e45, 60e62, 84e87 and 86e95%, respectively. Modification by network, as occurs with the use of wheat proteins, the textural
papain-based hydrolysis improved EA of the protein isolate from quality of brown rice breads was shown to improve following
109 m2/g to values in the range 150e185 m2/g, whereas the ES transglutaminase treatment (Renzetti, Dal Bello, & Arendt, 2008).
increased from 37 to 48 min upon papain treatment for 60 min. According to Renzetti et al. (2012) this effect is to be ascribed to the
Also, hydrolysis of the protein isolate using papain improved FC formation of large protein complexes, resulting from glutelin
from 70% to values in the range 118e151%, but decreased FS. polymerization, and the new and stronger hydrophobic in-
teractions among proteins induced by transglutaminase treatment.
5. Applications of rice proteins
6. Conclusions
Rice is generally recognized as a hypoallergenic food, being one
of the first solid foods to be introduced into the diet of infants, and Research has highlighted the nutritional properties and health
being used in most elimination diets for food allergy diagnostic benefits of proteins extracted from rice, a relatively low cost natural
programs in children and adults (Gastana ~duy, Cordano, & Graham, food. Since the interest of consumers worldwide for ingredients
1990). Therefore, rice protein-based formulas represent a suitable derived from natural sources such as plant proteins is ever-
alternative for children allergic to cow's milk. Infants diagnosed growing, increasing utilisation of rice proteins in food and phar-
with cow's milk allergy (CMA) are usually fed extensively hydro- maceutical applications is also expected. However, although prog-
lysed cow's milk formulas, soy protein-based formulas or amino ress has been made in understanding the composition, distribution,
acid-based formulas. However, these products present some processing and functional properties of rice proteins, more research
drawbacks. Despite being generally well tolerated, extensively is needed to thoroughly characterise and modify the functionality
hydrolysed cow's milk formulas (Committee on Nutrition of the of rice protein-based ingredients in order to widen the range of
American Academy of Pediatrics, 2000; Giampietro, Kjellman, applications of such ingredients and meet the needs of the food
Oldaeus, Wouters-Wesseling, & Businco, 2001; Kaczmarski, Wasi- processing and market sectors.
lewska, & Lasota, 2005; Klemola et al., 2002; Vandenplas et al.,
2007) and soy formulas (Klemola et al., 2002; Zeiger et al., 1999),
Acknowledgement
have the ability to cause allergic reactions in infants with CMA,
whereas poor palatability and high cost limit the use of amino acid-
The authors would like to thank Nestle for providing financial
based formulas, although they are non-allergic (Caffarelli et al.,
support for this study.
2010). A number of studies have shown that hydrolysed rice
protein-based formulas are tolerated by and nutritionally adequate
for infants with CMA (Agostoni et al., 2007; D'Auria et al., 2003; References
Fiocchi et al., 2006, 2003; Reche et al., 2010) and thus represent
Adebiyi, A. P., Adebiyi, A. O., Hasegawa, Y., Ogawa, T., & Muramoto, K. (2009a).
suitable alternatives to the aforementioned formulas. Furthermore, Isolation and characterization of protein fractions from deoiled rice bran. Eu-
a partially-hydrolysed rice protein-based formula fortified with ropean Food Research and Technology, 228, 391e401.
Adebiyi, A. P., Adebiyi, A. O., Jin, D. H., Ogawa, T., & Muramoto, K. (2008). Rice bran
lysine and threonine has been shown to support normal growth
protein-based edible films. International Journal of Food Science and Technology,
and plasma biochemistry when used as the exclusive source of 43, 476e483.
nutrition in healthy term infants during the first four months of life Adebiyi, A. P., Adebiyi, A. O., Ogawa, T., & Muramoto, K. (2007). Preparation and
(Lasekan, Koo, Walters, Neylan, & Luebbers, 2006). characterization of high-quality rice bran proteins. Journal of the Science of Food
and Agriculture, 87, 1219e1227.
The use of rice protein ingredients as supplements in sports Adebiyi, A. P., Adebiyi, A. O., Yamashita, J., Ogawa, T., & Muramoto, K. (2009b).
nutrition, as an alternative to the more commonly used casein, Purification and characterization of antioxidative peptides derived from rice
whey and soy proteins, is also increasing, and some studies have bran protein hydrolysates. European Food Research and Technology, 228,
553e563.
shown that rice protein concentrates can be used as value-added Agboola, S., Ng, D., & Mills, D. (2005). Characterisation and functional properties of
ingredients in the production of bread (Jiamyangyuen et al., Australian rice protein isolates. Journal of Cereal Science, 41, 283e290.
2005), biscuits (Yadav et al., 2011) and edible films (Adebiyi, Agostoni, C., Fiocchi, A., Riva, E., Terracciano, L., Sarratud, T., Martelli, A., et al.
(2007). Growth of infants with IgE-mediated cow's milk allergy fed different
Adebiyi, Jin, Ogawa, & Muramoto, 2008; Shih, 1996) with formulas in the complementary feeding period. Pediatric Allergy and Immu-
improved nutritional and functional properties. nology, 18, 599e606.
The generally low solubility in water of intact rice protein in- Aletor, O., Oshodi, A. A., & Ipinmoroti, K. (2002). Chemical composition of common
leafy vegetables and functional properties of their leaf protein concentrates.
gredients limits their potential applications to products that do not Food Chemistry, 78, 63e68.
require high solubility of the protein ingredients, e.g., meat ana- Anderson, A., Hettiarachchy, N. S., & Ju, Z. Y. (2001). Physicochemical properties of
logues, baked goods, breakfast cereals, protein bars and pet food. pronase-treated rice glutelin. Journal of the American Oil Chemists’ Society, 78,
1e6.
However, the functionality of rice proteins may be improved by
Ansharullah, Hourigan, J. A., & Chesterman, C. F. (1997). Application of carbohy-
means of enzymatic hydrolysis, allowing for the use of these pro- drases in extracting protein from rice bran. Journal of the Science of Food and
tein ingredients in a wider range of food products including soups, Agriculture, 74, 141e146.
sauces, salad dressings, whipped toppings, coffee creamers, forti- Arntfield, S. D., & Murray, E. D. (1981). The influence of processing parameters on
food protein functionality. I. Differential scanning calorimetry as an indicator of
fied beverages, enteral and clinical nutrition products, as well as protein denaturation. Canadian Institute of Food Science and Technology Journal,
pharmaceuticals. 14, 289e294.
10 L. Amagliani et al. / Trends in Food Science & Technology 64 (2017) 1e12
Bandyopadhyay, K., Misra, G., & Ghosh, S. (2008). Preparation and characterisation Chemistry, 54, 3663e3667.
of protein hydrolysates from Indian defatted rice bran meal. Journal of Oleo Hamada, J. S. (1997). Characterization of protein fractions of rice bran to devise
Science, 57, 47e52. effective methods of protein solubilization. Cereal Chemistry, 74, 662e668.
Bechtel, D. B., & Juliano, B. O. (1980). formation of protein bodies in the starchy Hamada, J. S. (1999). Use of proteases to enhance solubilization of rice bran pro-
endosperm of rice (Oryza sativa L.): A re-investigation. Annals of Botany, 45, teins. Journal of Food Biochemistry, 23, 307e321.
503e509. Hamada, J. S. (2000). Characterization and functional properties of rice bran pro-
Bechtel, D. B., & Pomeranz, Y. (1978). Ultrastructure of the mature ungerminated teins modified by commercial exoproteases and endoproteases. Journal of Food
rice (Oryza sativa) caryopsis. The starchy endosperm. American Journal of Bot- Science, 65, 305e310.
any, 65, 684e691. Hamaker, B. R. (1994). The influence of rice protein on rice quality. In W. E. Marshall,
Blakeney, A. (1984). Rice grain quality. In A. Currey (Ed.), Rice growing in new south & J. I. Wadsworth (Eds.), Rice science and technology (pp. 177e194). New York,
wales (pp. 1e5). Yanco, Australia: Department of Agriculture New South Wales NY: Marcel Dekker, Inc.
and the Rice Research Committee. Han, S. W., Chee, K. M., & Cho, S. J. (2015). Nutritional quality of rice bran protein in
Burris, R. L., Xie, C. H., Thampi, P., Wu, X., Melnyk, S. B., & Nagarajan, S. (2010). comparison to animal and vegetable protein. Food Chemistry, 172, 766e769.
Dietary rice protein isolate attenuates atherosclerosis in apoE-deficient mice by Hata, S., Wiboonsirikul, J., Maeda, A., Kimura, Y., & Adachi, S. (2008). Extraction of
upregulating antioxidant enzymes. Atherosclerosis, 212, 107e115. defatted rice bran by subcritical water treatment. Biochemical Engineering
Caffarelli, C., Baldi, F., Bendandi, B., Calzone, L., Marani, M., & Pasquinelli, P. (2010). Journal, 40, 44e53.
Cow's milk protein allergy in children: A practical guide. Italian Journal of Pe- Helm, R. M., & Burks, A. W. (1996). Hypoallergenicity of rice protein. Cereal Foods
diatrics, 36, 1e7. World, 41, 839e843.
Cagampang, G. B., Cruz, L. J., Espiritu, S. G., Santiago, R. G., & Juliano, B. O. (1966). Herrero, M., Cifuentes, A., & Iban ~ ez, E. (2006). Sub- and supercritical fluid extraction
Studies on the extraction and composition of rice proteins. Cereal Chemistry, 43, of functional ingredients from different natural sources: Plants, food-by-
145e155. products, algae and microalgae. Food Chemistry, 98, 136e148.
Cao, X., Wen, H., Li, C., & Gu, Z. (2009). Differences in functional properties and Hibino, T., Kidzu, K., Masumura, T., Ohtsuki, K., Tanaka, K., Kawabata, M., et al.
biochemical characteristics of congenetic rice proteins. Journal of Cereal Science, (1989). Amino acid composition of rice prolamin polypeptides. Agricultural and
50, 184e189. Biological Chemistry, 53, 513e518.
Champagne, E. T., Wood, D. F., Juliano, B. O., & Bechtel, D. B. (2004). The rice grain Hou, L., Zhu, Y., & Li, Q. (2010). Characterization and preparation of broken rice
and its gross composition. In E. T. Champagne (Ed.), Rice: Chemistry and tech- proteins modified by proteases. Food Technology and Biotechnology, 48, 50e55.
nology (3rd ed., pp. 77e107). St. Paul, MN: American Association of Cereal Huppertz, T. (2010). Foaming properties of milk: A review of the influence of
Chemists. composition and processing. International Journal of Dairy Technology, 63,
Chandi, G. K., & Sogi, D. S. (2007). Functional properties of rice bran protein con- 477e488.
centrates. Journal of Food Engineering, 79, 592e597. Iwasaki, T., Shibuya, N., Suzuki, T., & Chikubu, S. (1982). Gel filtration and electro-
Chanput, W., Theerakulkait, C., & Nakai, S. (2009). Antioxidative properties of phoresis of soluble rice proteins extracted from long, medium, and short grain
partially purified barley hordein, rice bran protein fractions and their hydro- varieties. Cereal Chemistry, 59, 192e195.
lysates. Journal of Cereal Science, 49, 422e428. Jiamyangyuen, S., Srijesdaruk, V., & Harper, W. J. (2005). Extraction of rice bran
Childs, N. W. (2004). Production and utilization of rice. In E. T. Champagne (Ed.), protein concentrate and its application in bread. Songklanakarin Journal of Sci-
Rice: Chemistry and technology (3rd ed., pp. 1e23). St. Paul, MN: American As- ence and Technology, 27, 55e64.
sociation of Cereal Chemists. Ju, Z. Y., Hettiarachchy, N. S., & Rath, N. (2001). Extraction, denaturation and hy-
Chittapalo, T., & Noomhorm, A. (2009). Ultrasonic assisted alkali extraction of drophobic properties of rice flour proteins. Journal of Food Science, 66, 229e232.
protein from defatted rice bran and properties of the protein concentrates. Juliano, B. O. (1985). Polysaccharides, proteins, and lipids of rice. In B. O. Juliano
International Journal of Food Science and Technology, 44, 1843e1849. (Ed.), Rice: Chemistry and technology (2nd ed., pp. 59e174). St. Paul, MN:
Chrastil, J., & Zarins, Z. M. (1992). Influence of storage on peptide subunit compo- American Association of Cereal Chemists.
sition of rice oryzenin. Journal of Agricultural and Food Chemistry, 40, 927e930. Juliano, B. O., & Bechtel, D. B. (1985). The rice grain and its gross composition. In
Coffman, W. R., & Juliano, B. O. (1987). Rice. In R. A. Olson, & K. G. Frey (Eds.), B. O. Juliano (Ed.), Rice: Chemistry and technology (2nd ed., pp. 17e57). St. Paul,
Nutritional quality of cereal Grains: Genetic and agronomic improvement (pp. MN: American Association of Cereal Chemists.
101e131). American Society of Agronomy, Crop Science Society of America, Soil Kaczmarski, M., Wasilewska, J., & Lasota, M. (2005). Hypersensitivity to hydrolyzed
Science Society of America. cow's milk protein formula in infants and young children with atopic eczema/
Committee on Nutrition of the American Academy of Pediatrics. (2000). Hypoal- dermatitis syndrome with cow's milk protein allergy. Roczniki Akademii
lergenic infant formulas. Pediatrics, 106, 346e349. Medycznej w Białymstoku, 50, 274e278.
Damodaran, S. (1994). Structure-function relationship of food proteins. In Kannan, A., Hettiarachchy, N. S., Johnson, M. G., & Nannapaneni, R. (2008). Human
N. S. Hettiarachchy, & G. R. Ziegler (Eds.), Protein functionality in food systems colon and liver cancer cell proliferation inhibition by peptide hydrolysates
(pp. 1e37). New York, NY: Marcel Dekker, Inc. derived from heat-stabilized defatted rice bran. Journal of Agricultural and Food
Day, L. (2013). Proteins from land plants - potential resources for human nutrition Chemistry, 56, 11643e11647.
and food security. Trends in Food Science & Technology, 32, 25e42. Kannan, A., Hettiarachchy, N. S., Lay, J. O., & Liyanage, R. (2010). Human cancer cell
D'Auria, E., Sala, M., Lodi, F., Radaelli, G., Riva, E., & Giovannini, M. (2003). Nutri- proliferation inhibition by a pentapeptide isolated and characterized from rice
tional value of a rice-hydrolysate formula in infants with cow's milk protein bran. Peptides, 31, 1629e1634.
allergy: A randomized pilot study. Journal of International Medical Research, 31, Kannan, A., Hettiarachchy, N. S., & Mahedevan, M. (2012). Peptides derived from
215e222. rice bran protect cells from obesity and Alzheimer's disease. International
Eggum, B. O. (1979). The nutritional value of rice in comparison with other cereals. Journal of Biomedical Research, 3, 131e135.
In Proceedings of the workshop on chemical aspects of rice grain quality (pp. Kannan, A., Hettiarachchy, N. S., & Narayan, S. (2009). Colon and breast anti-cancer
91e111). Los Ban ~ os, Laguana, Philippines: International Rice Research Institute. effects of peptide hydrolysates derived from rice bran. The Open Bioactive
Fabian, C., & Ju, Y. H. (2011). A review on rice bran protein: Its properties and Compounds Journal, 2, 17e20.
extraction methods. Critical Reviews in Food Science and Nutrition, 51, 816e827. Khan, S. H., Butt, M. S., Sharif, M. K., Sameen, A., Mumtaz, S., & Sultan, M. T. (2011).
Fiocchi, A., Restani, P., Bernardini, R., Lucarelli, S., Lombardi, G., Magazzù, G., et al. Functional properties of protein isolates extracted from stabilized rice bran by
(2006). A hydrolysed rice-based formula is tolerated by children with cow's microwave, dry heat and parboiling. Journal of Agricultural and Food Chemistry,
milk allergy: A multi-centre study. Clinical & Experimental Allergy, 36, 311e316. 59, 2416e2420.
Fiocchi, A., Travaini, M., D'Auria, E., Banderali, G., Bernardo, L., & Riva, E. (2003). Klemola, T., Vanto, T., Juntunen-Backman, K., Kalimo, K., Korpela, R., & Varjonen, E.
Tolerance to a rice hydrolysate formula in children allergic to cow's milk and (2002). Allergy to soy formula and to extensively hydrolyzed whey formula in
soy. Clinical & Experimental Allergy, 33, 1576e1580. infants with cow's milk allergy: A prospective, randomized study with a follow-
Gastana ~duy, A., Cordano, A., & Graham, G. G. (1990). Acceptability, tolerance, and up to the age of 2 years. Journal of Pediatrics, 140, 219e224.
nutritional value of a rice-based infant formula. Journal of Pediatric Gastroen- Krishnan, H. B., & Okita, T. W. (1986). Structural relationship among the rice glutelin
terology and Nutrition, 11, 240e246. polypeptides. Plant Physiology, 81, 748e753.
Giampietro, P. G., Kjellman, N. I. M., Oldaeus, G., Wouters-Wesseling, W., & Krishnan, H. B., White, J. A., & Pueppke, S. G. (1992). Characterization and locali-
Businco, L. (2001). Hypoallergenicity of an extensively hydrolysed whey for- zation of rice (Oryza sativa L.) seed globulins. Plant Science, 81, 1e11.
mula. Pediatric Allergy and Immunology, 12, 83e86. Kubota, M., Saito, Y., Masamura, T., Kumagai, T., Watanabe, R., Fujimura, S., et al.
Gnanasambandam, R., & Hettiarachchy, N. S. (1995). Protein concentrates from (2010). Improvement in the in vivo digestibility of rice protein by alkali
unstabilized and stabilized rice bran: Preparation and properties. Journal of extraction is due to structural changes in prolamin/protein body-I particle.
Food Science, 60, 1066e1069. Bioscience, Biotechnology, and Biochemistry, 74, 614e619.
Guo, X., Zhang, J., Ma, Y., & Tian, S. (2013). Optimization of limited hydrolysis of Kumagai, T., Kawamura, H., Fuse, T., Watanabe, T., Saito, Y., Masamura, T., et al.
proteins in rice residue and characterization of the functional properties of the (2006). Production of rice protein by alkaline extraction improves its di-
products. Journal of Food Processing and Preservation, 37, 245e253. gestibility. Journal of Nutritional Science and Vitaminology, 52, 467e472.
Hager, A. S., Wolter, A., Jacob, F., Zannini, E., & Arendt, E. K. (2012). Nutritional Kumagai, T., Watanabe, R., Saito, M., Watanabe, T., Kubota, M., & Kadowaki, M.
properties and ultra-structure of commercial gluten free flours from different (2009). Superiority of alkali-extracted rice protein in bioavailability to starch
botanical sources compared to wheat flours. Journal of Cereal Science, 56, degraded rice protein comes from digestion of prolamin in growing rats. Journal
239e247. of Nutritional Science and Vitaminology, 55, 170e177.
Haghighat Khajavi, S., Ota, S., Kimura, Y., & Adachi, S. (2006). Kinetics of maltooli- Lakkakula, N. R., Lima, M., & Walker, T. (2004). Rice bran stabilization and rice bran
gosaccharide hydrolysis in subcritical water. Journal of Agricultural and Food oil extraction using ohmic heating. Bioresource Technology, 92, 157e161.
L. Amagliani et al. / Trends in Food Science & Technology 64 (2017) 1e12 11
Lasekan, J. B., Koo, W. W. K., Walters, J., Neylan, M., & Luebbers, S. (2006). Growth, Sereewatthanawut, I., Prapintip, S., Watchiraruji, K., Goto, M., Sasaki, M., &
tolerance and biochemical measures in healthy infants fed a partially hydro- Shotipruk, A. (2008). Extraction of protein and amino acids from deoiled rice
lysed rice protein-based formula: A randomized, blinded, prospective trial. bran by subcritical water hydrolysis. Bioresource Technology, 99, 555e561.
Journal of the American College of Nutrition, 25, 12e19. Shewry, P. R., & Casey, R. (1999). Seed proteins. Kluwer Academic Publishers.
Lasztity, R. (1995). Rice proteins. In R. Lasztity (Ed.), The chemistry of cereal proteins Shewry, P. R., & Halford, N. G. (2002). Cereal seed storage proteins: Structures,
(2nd ed., pp. 249e273). Boca Raton, FL: CRC Press, Inc. properties and role in grain utilization. Journal of Experimental Botany, 53,
Li, G. H., Qu, M. R., Wan, J. Z., & You, J. M. (2007). Antihypertensive effect of rice 947e958.
protein hydrolysate with in vitro angiotensin I-converting enzyme inhibitory Shih, F. F. (1996). Edible films from rice protein concentrate and pullulan. Cereal
activity in spontaneously hypertensive rats. Asia Pacific Journal of Clinical Chemistry, 73, 406e409.
Nutrition, 16, 275e280. Shih, F. F. (2003). An update on the processing of high-protein rice products.
Li, X., Xiong, H., Yang, K., Peng, D., Peng, H., & Zhao, Q. (2012). Optimization of the Nahrung/Food, 47, 420e424.
biological processing of rice dregs into nutritional peptides with the aid of Shih, F. F. (2004). Rice proteins. In E. T. Champagne (Ed.), Rice: Chemistry and
trypsin. Journal of Food Science and Technology, 49, 537e546. technology (3rd ed., pp. 143e162). St. Paul, MN: American Association of Cereal
Luthe, D. S. (1983). Storage protein accumulation in developing rice (Oryza sativa L.) Chemists.
seeds. Plant Science Letters, 32, 147e158. Shih, F. F., Champagne, E. T., Daigle, K., & Zarins, Z. (1999). Use of enzymes in the
Mawal, Y. R., Mawal, M. R., & Ranjekar, P. K. (1987). Biochemical and immunological processing of protein products from rice bran and rice flour. Nahrung/Food, 43,
characterization of rice albumin. Bioscience Reports, 7, 1e9. 14e18.
Moroni, A. V., Iametti, S., Bonomi, F., Arendt, E. K., & Dal Bello, F. (2010). Solubility of Shih, F. F., & Daigle, K. W. (2000). Preparation and characterization of rice protein
proteins from non-gluten cereals: A comparative study on combinations of isolates. Journal of the American Oil Chemists’ Society, 77, 885e889.
solubilising agents. Food Chemistry, 121, 1225e1230. Sugimoto, T., Tanaka, K., & Kasai, Z. (1986). Molecular species in the protein body II
Muthayya, S., Sugimoto, J. D., Montgomery, S., & Maberly, G. F. (2014). An overview (PB-II) of developing rice endosperm. Agricultural and Biological Chemistry, 50,
of global rice production, supply, trade, and consumption. Annals of the New 3031e3035.
York Academy of Sciences, 1324, 7e14. Sunphorka, S., Chavasiri, W., Oshima, Y., & Ngamprasertsith, S. (2012). Kinetic
Nielsen, P. M. (1997). Functionality of protein hydrolysates. In S. Damodaran, & studies on rice bran protein hydrolysis in subcritical water. Journal of Super-
A. Paraf (Eds.), Food proteins and their applications (pp. 443e472). New York, NY: critical Fluids, 65, 54e60.
Marcel Dekker, Inc. Tanaka, K., Sugimoto, T., Ogawa, M., & Kasai, Z. (1980). Isolation and characterization
Ogawa, M., Kumamaru, T., Satoh, H., Iwata, N., Omura, T., Kasai, Z., et al. (1987). of two types of protein bodies in the rice endosperm. Agricultural and Biological
Purification of protein body-I of rice seed and its polypeptide composition. Plant Chemistry, 44, 1633e1639.
and Cell Physiology, 28, 1517e1527. Tang, S., Hettiarachchy, N. S., & Shellhammer, T. H. (2002). Protein extraction from
Ogawa, M., Kumamaru, T., Satoh, H., Omura, T., Park, T., Shintaku, K., et al. (1989). heat-stabilized defatted rice bran. 1. Physical processing and enzyme treat-
Mutants for rice storage proteins: 2. Isolation and characterization of protein ments. Journal of Agricultural and Food Chemistry, 50, 7444e7448.
bodies from rice mutants. Theoretical and Applied Genetics, 78, 305e310. USDA. (August 2015). Grain: World markets and trade. Washington, DC: United
Orthoefer, F. T., & Eastman, J. (2004). Rice bran and oil. In E. T. Champagne (Ed.), States Department of Agriculture, Foreign Agricultural Service.
Rice: Chemistry and technology (3rd ed., pp. 569e593). St. Paul, MN: American Vandenplas, Y., Brueton, M., Dupont, C., Hill, D., Isolauri, E., Koletzko, S., et al. (2007).
Association of Cereal Chemists. Guidelines for the diagnosis and management of cow's milk protein allergy in
Osborne, T. B. (1924). The vegetable proteins. London, UK: Longmans, Green and Co. infants. Archives of Disease in Childhood, 92, 902e908.
Otterburn, M. S. (1989). Protein crosslinking. In R. D. Phillips, & J. W. Finley (Eds.), Villareal, R. M., & Juliano, B. O. (1981). Properties of albumins of milled rice.
Protein quality and the effects of processing. New York, NY: Marcel Dekker, Inc. Phytochemistry, 20, 1785e1789.
Padhye, V. W., & Salunkhe, D. K. (1979). Extraction and characterization of rice Wang, M., Hettiarachchy, N. S., Qi, M., Burks, W., & Siebenmorgen, T. (1999). Prep-
proteins. Cereal Chemistry, 56, 389e393. aration and functional properties of rice bran protein isolate. Journal of Agri-
Panyam, D., & Kilara, A. (1996). Enhancing the functionality of food proteins by cultural and Food Chemistry, 47, 411e416.
enzymatic modification. Trends in Food Science & Technology, 7, 120e125. Watchararuji, K., Goto, M., Sasaki, M., & Shotipruk, A. (2008). Value-added
Paraman, I., Hettiarachchy, N. S., & Schaefer, C. (2008). Preparation of rice endo- subcritical water hydrolysate from rice bran and soybean meal. Bioresource
sperm protein isolate by alkali extraction. Cereal Chemistry, 85, 76e81. Technology, 99, 6207e6213.
Paraman, I., Hettiarachchy, N. S., Schaefer, C., & Beck, M. I. (2007). Hydrophobicity, Wen, T. N., & Luthe, D. S. (1985). Biochemical characterization of rice glutelin. Plant
solubility, and emulsifying properties of enzyme-modified rice endosperm Physiology, 78, 172e177.
protein. Cereal Chemistry, 84, 343e349. Wiboonsirikul, J., Kimura, Y., Kadota, M., Morita, H., Tsuno, T., & Adachi, S. (2007).
Pearce, K. N., & Kinsella, J. E. (1978). Emulsifying properties of proteins: Evaluation Properties of extracts from defatted rice bran by its subcritical water treatment.
of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26, Journal of Agricultural and Food Chemistry, 55, 8759e8765.
716e723. Wiboonsirikul, J., Kimura, Y., Kanaya, Y., Tsuno, T., & Adachi, S. (2008). Production
Piorkowski, D. T., & McClements, D. J. (2014). Beverage emulsions: Recent de- and characterization of functional substances from a by-product of rice bran oil
velopments in formulation, production, and applications. Food Hydrocolloids, and protein production by a compressed hot water treatment. Bioscience,
42, 5e41. Biotechnology, and Biochemistry, 72, 384e392.
Prakash, J., & Ramanatham, G. (1994). Effect of stabilization of rice bran on the Xia, N., Wang, J. M., Gong, Q., Yang, X. Q., Yin, S. W., & Qi, J. R. (2012a). Character-
extractability and recovery of proteins. Nahrung/Food, 38, 87e95. ization and in vitro digestibility of rice protein prepared by enzyme-assisted
Ramezanzadeh, F. M., Rao, R. M., Prinyawiwatkul, W., Marshall, W. E., & microfluidization: Comparison to alkaline extraction. Journal of Cereal Science,
Windhauser, M. (2000). Effects of microwave heat, packaging, and storage 56, 482e489.
temperature on fatty acid and proximate composition in rice bran. Journal of Xia, N., Wang, J., Yang, X., Yin, S., Qi, J., Hu, L., et al. (2012b). Preparation and
Agricultural and Food Chemistry, 48, 464e467. characterization of protein from heat-stabilized rice bran using hydrothermal
Reche, M., Pascual, C., Fiandor, A., Polanco, I., Rivero-Urgell, M., Chifre, R., et al. cooking combined with amylase pretreatment. Journal of Food Engineering, 110,
(2010). The effect of a partially hydrolysed formula based on rice protein in the 95e101.
treatment of infants with cow's milk protein allergy. Pediatric Allergy and Yadav, R. B., Yadav, B. S., & Chaudhary, D. (2011). Extraction, characterization and
Immunology, 21, 577e585. utilization of rice bran protein concentrate for biscuit making. British Food
Renzetti, S., Behr, J., Vogel, R. F., Barbiroli, A., Iametti, S., Bonomi, F., et al. (2012). Journal, 113, 1173e1182.
Transglutaminase treatment of brown rice flour: A chromatographic, electro- Yamagata, H., Sugimoto, T., Tanaka, K., & Kasai, Z. (1982). Biosynthesis of storage
phoretic and spectroscopic study of protein modifications. Food Chemistry, 131, proteins in developing rice seeds. Plant Physiology, 70, 1094e1100.
1076e1085. Yang, L., Chen, J. H., Lv, J., Wu, Q., Xu, T., Zhang, H., et al. (2012a). Rice protein im-
Renzetti, S., Dal Bello, F., & Arendt, E. K. (2008). Microstructure, fundamental proves adiposity, body weight and reduces lipids level in rats through modifi-
rheology and baking characteristics of batters and breads from different gluten- cation of triglyceride metabolism. Lipids in Health and Disease, 11, 24e33.
free flours treated with a microbial transglutaminase. Journal of Cereal Science, Yang, L., Chen, J. H., Xu, T., Qiu, W., Zhang, Y., Zhang, L. W., et al. (2011). Rice protein
48, 33e45. extracted by different methods affects cholesterol metabolism in rats due to its
Robert, L. S., Nozzolillo, C., & Altosaar, I. (1985). Homology between rice glutelin and lower digestibility. International Journal of Molecular Sciences, 12, 7594e7608.
oat 12 S globulin. Biochimica et Biophysica Acta, 829, 19e26. Yang, L., Kumagai, T., Kawamura, H., Watanabe, T., Kubota, M., Fujimura, S., et al.
Romero, A., Beaumal, V., David-Briand, E., Cordobes, F., Guerrero, A., & Anton, M. (2007). Effects of rice proteins from two cultivars, Koshihikari and Shunyo, on
(2012). Interfacial and emulsifying behaviour of rice protein concentrate. Food cholesterol and triglyceride metabolism in growing and adult rats. Bioscience,
Hydrocolloids, 29, 1e8. Biotechnology, and Biochemistry, 71, 694e703.
Sarker, S. C., Ogawa, M., Takahashi, M., & Asada, K. (1986). The processing of a 57- Yang, T., Zhu, H., Zhou, H., Lin, Q., Li, W., & Liu, J. (2012b). Rice protein hydrolysate
kDa precursor peptide to subunits of rice glutelin. Plant and Cell Physiology, 27, attenuates hydrogen peroxide induced apoptosis of myocardiocytes H9c2
1579e1586. through the Bcl-2/Bax pathway. Food Research International, 48, 736e741.
Sayre, R. N., Saunders, R. M., Enochian, R. V., Schultz, W. G., & Beagle, E. C. (1982). Young, V. R., & Pellett, P. L. (1994). Plant proteins in relation to human protein and
Review of rice bran stabilization systems with emphasis on extrusion cooking. amino acid nutrition. American Journal of Clinical Nutrition, 59, 1203Se1212S.
Cereal Foods World, 27, 317e322. Zarins, Z., & Chrastil, J. (1992). Separation and purification of rice oryzenin subunits
Schwenke, K. D. (1997). Enzyme and chemical modification of proteins. In by anion-exchange and gel-permeation chromatography. Journal of Agricultural
S. Damodaran, & A. Paraf (Eds.), Food proteins and their applications (pp. and Food Chemistry, 40, 1599e1601.
393e423). New York, NY: Marcel Dekker, Inc. Zeiger, R. S., Sampson, H. A., Bock, S. A., Burks, A. W., Harden, K., Noone, S., et al.
12 L. Amagliani et al. / Trends in Food Science & Technology 64 (2017) 1e12
(1999). Soy allergy in infants and children with IgE-associated cow's milk al- acid sequence of a polypeptide from the glutelin fraction of rice grains; ho-
lergy. Journal of Pediatrics, 134, 614e622. mology to pea legumin. FEBS Letters, 162, 96e102.
Zhang, H., Bartley, G. E., Mitchell, C. R., Zhang, H., & Yokoyama, W. (2011). Lower Zhao, Q., Selomulya, C., Xiong, H., Chen, X. D., Ruan, X., Wang, S., et al. (2012a).
weight gain and hepatic lipid content in hamsters fed high fat diets supple- Comparison of functional and structural properties of native and industrial
mented with white rice protein, brown rice protein, soy protein, and their process-modified proteins from long-grain indica rice. Journal of Cereal Science,
hydrolysates. Journal of Agricultural and Food Chemistry, 59, 10927e10933. 56, 568e575.
Zhang, J., Zhang, H., Wang, L., Guo, X., Wang, X., & Yao, H. (2009). Antioxidant ac- Zhao, Q., Xiong, H., Selomulya, C., Chen, X. D., Huang, S., Ruan, X., et al. (2013).
tivities of the rice endosperm protein hydrolysate: Identification of the active Effects of spray drying and freeze drying on the properties of protein isolate
peptide. European Food Research and Technology, 229, 709e719. from rice dreg protein. Food and Bioprocess Technology, 6, 1759e1769.
Zhang, J., Zhang, H., Wang, L., Guo, X., Wang, X., & Yao, H. (2010). Isolation and Zhao, Q., Xiong, H., Selomulya, C., Chen, X. D., Zhong, H., Wang, S., et al. (2012b).
identification of antioxidative peptides from rice endosperm protein enzymatic Enzymatic hydrolysis of rice dreg protein: Effects of enzyme type on the
hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS. Food functional properties and antioxidant activities of recovered proteins. Food
Chemistry, 119, 226e234. Chemistry, 134, 1360e1367.
Zhao, W. M., Gatehouse, J. A., & Boulter, D. (1983). The purification and partial amino