Plant-Based Proteins

C H A P T E R

4 Plant-Based Proteins Rene´ Renato Balandra´n-Quintana1, Ana Marı´a Mendoza-Wilson1, Gabriela Ramos-Clamont Montfort2 and ´ ngel Huerta-Ocampo3 Jose´ A 1

Center for Research in Food and Development, A.C. Coordination of Technology of Foods from Vegetal Origin, Hermosillo, Sonora, Mexico 2Center for Research in Food and Development, A.C. Coordination of Food Science, Hermosillo, Sonora, Mexico 3 CONACYT-Center for Research in Food and Development, A.C. Coordination of Food Science, Hermosillo, Sonora, Mexico O U T L I N E

4.1 General Introduction

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4.2 Importance of Proteins in Human Nutrition and Food Processing

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4.3 Plant-Based Proteins in the Sustainability Context

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4.4 Properties and Extraction of Plant Proteins

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4.4.1 Cereal and Pseudocereal Proteins 103 4.4.2 Proteins from By-Products of Plant Oil Refining Industry 111 4.4.3 Other Sources of Plant Proteins 118 4.5 Concluding Remarks

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References

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4.1 GENERAL INTRODUCTION Proteins are important biomolecules because of their essential functions for life (Berg et al., 2002) and attributes they provide to many food systems (Li-Chan and Lacroix, 2018). Proteins of animal origin are of higher quality than plant proteins, due to their high digestibility, better amino acid score (AAS), and greater water solubility. An increasing population demands to consume more meat (Tilman and Clark, 2014) but meeting this demand implicates strong environmental impacts so the global food system is considered among

Proteins: Sustainable Source, Processing and Applications DOI: https://doi.org/10.1016/B978-0-12-816695-6.00004-0

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© 2019 Elsevier Inc. All rights reserved.

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the goals for sustainable development (Chaudhary et al., 2018). A solution to the problem of protein sustainability could be the shift to diets based on plant protein (Day, 2013). Digestibility and the contribution of essential amino acids, which in principle should be the most important drawbacks, can be solved by combining proteins from different plant sources (Mariotti, 2017). However, the biggest challenge is cultural (Macdiarmid et al., 2016) as the population is reluctant to replace animal proteins with plant ones. Since the act of eating is predominantly sensory, the academic and industrial sectors have two important challenges ahead: identifying alternative sources of proteins that meet the nutritional expectations and innovating to offer sensory-acceptable products (Day, 2013; Fritsch et al., 2017). In this chapter, the concept of sustainability in the food context is briefly addressed and updated scientific information on nutritional aspects, extraction, properties, and potential uses of conventional and nonconventional sources of vegetable protein is presented. The objective of gathering this information is to serve as a guide for technologists and academics interested in entering the field of protein sustainability.

4.2 IMPORTANCE OF PROTEINS IN HUMAN NUTRITION AND FOOD PROCESSING Amino acids determine both the structure and function of proteins and so their biological value (Berg et al., 2002). Eleven of the 20 amino acids found in proteins are synthesized in the cells of the human body. The remaining nine are not synthesized and so are essential or indispensable (Reeds, 2000), and must be provided through the diet (Tessari et al., 2016). Indispensable amino acids, whose content in a food is less than the optimum recommended level, are known as limiting amino acids (Friedman, 1996). Protein quality is measured in several ways. The AAS predicts the efficiency to meet the recommended levels of essential amino acids and is estimated for different age groups according to the recommended dietary protein intake (https://www.nal.usda.gov/fnic/ protein-and-amino-acids). An AAS greater than or equal to 100 (often the value is truncated to 100) indicates that the protein completely satisfies the recommended levels of essential amino acids; however, this does not take into account their bioavailability. The latter is included in the protein digestibility-corrected amino acid score (PDCAAS), which is calculated by multiplying the AAS by the digestibility of the protein (Schaafsma, 2000). Often, in literature PDCAAS values are indicated as a fraction. Here were converted to percentage in order to homogenize style, when necessary. Since a good protein digestibility does not mean bioavailability of all the indispensable amino acids (Schaafsma, 2000), the digestible indispensable amino acid score (DIAAS) was suggested as a new measure of protein quality (FAO, 2013). In DIAAS, each amino acid is considered a nutrient, so the individual digestibility of essential amino acids is taken into account. It is calculated by multiplying by a hundred the quotient obtained by dividing the content of the indispensable amino acid digestible in the dietary protein by the content of the same AA in the reference protein. A DIAAS 5 100% indicates a quality equal to that of the reference protein. In general, proteins of animal origin have a better score of essential amino acids and greater digestibility than those of plant origin, which is why they are used as reference proteins. Tables 4.1 and 4.2 show a comparison between

PROTEINS: SUSTAINABLE SOURCE, PROCESSING AND APPLICATIONS

TABLE 4.1 Reported Values for Protein Content, Indispensable Amino Acids (IAA) Profile, Amino Acid Score (AAS), Protein Digestibility Corrected Amino Acid Score (PDCAAS), and Digestible Indispensable Amino Acid Score (DIAAS) of Representative Proteins From Plant Origin Corn (white, raw)

Wheat (hard winter)

Rice (white, raw)

Barley (pearled, raw)

Sorghum (raw)

Quinoa (raw)

Soy (protein isolate)

Peas (cooked)

Kidney beans (cooked)

Peanuts (roasted)

9.4a

12.6a

7.1a

9.9a

9.8d

14.1a

92.7e

8.3a

8.7a

23.7a

Tryptophan

713a

1270a

1169a

1667a

510d

1184a

1402e

1120a

1195a

970a

Threonine

3766a

2897a

3592a

3404a

2959d

2986a

3614e

3566a

3667a

3422a

Isoleucine

3585a

3635a

4338a

3657a

3776d

3574a

4725e

4145a

4713a

3515a

Leucine

12287a

6778a

8296a

6798a

1265d

5957a

7961e

7205a

8460a

6477a

Lysine

2819a

2659a

3634a

3727a

2041d

5433a

6138e

7253a

6977a

3586a

a

a

a

a

d

a

e

a

a

2511a

Protein (g/100 g) IAA (mg/100 g prot)

SAA

3904

AAA

9000a

Valine

4151

4423

4131

3061

3631

7770a

8718a

8485a

7856d

6099a

8813e

7542a

8230a

8819a

5074a

4413a

6127a

4909a

4694d

4213a

4768e

4747a

5747a

4190a

Histidine

3053a

2262a

2366a

2253a

2245d

2887a

2600e

2446a

2736a

2527a

AAS

55a

52a

71a

73a

40a

106a

96c

102a%

89a

70a

PDCAAS_(%)

59.9j

42b

63g

61l

16-24i

79k

91b

60f

65f

51f

DIAAS (%)

48d

43d

64d

51d

29d

--

99.6h

58f

59f

43f

a

2415

2554

2230

From Nutrition Data. Available from: https://nutritiondata.self.com. From Hess, J., Slavin, J., 2016. Defining “protein” foods. Nutr. Today 51(3), 117 120, (Hess and Slavin, 2016). c From Schaafsma, G., 2000. The protein digestibility-corrected amino acid score. J. Nutr. 130 (7), 1865s 1867s, (Schaafsma, 2000). d From Cervantes-Pahm, S., Liu, Y., Stein, H., 2014. Digestible indispensable amino acid score and digestible amino acids in eight cereal grains. Br. J. Nutr. 111(9), 1663-1672, (Cervantes-Pahm et al., 2014). e From Mathai, J., Liu, Y., Stein, H., 2017. Values for digestible indispensable amino acid scores (DIAAS) for some dairy and plant proteins may better describe protein quality than values calculated using the concept for protein digestibility-corrected amino acid scores (PDCAAS). Br. J. Nutr. 117(4), 490 499, (Mathai et al., 2017). f From Rutherfurd, S.M., Fanning, A.C., Miller, B.J., Mougha, P.J., 2015. Protein digestibility-corrected amino acid scores and digestible indispensable amino acid scores differentially describe protein quality in growing male rats. J. Nutr.145, 372 379, (Rutherfurd et al., 2015). g From Sung-Wook H., Kyu-Man, C., Seong-Jun, C., 2015. Nutritional quality of rice bran protein in comparison to animal and vegetable protein. Food Chem. 172, 766 769, (Sung-Wook et al., 2015); (Determined in endosperm; in rice bran, PDCAAS reaches 90%). h From Ertl, P., Knaus, W., Zollitsch, W., 2016. An approach to including protein quality when assessing the net contribution of livestock to human food supply. Animal 10 (11), 1883 1889, (Ertl et al., 2016). i From da Silva, L.S., Jung, R., Zhao, Z.-Y., Glassman, K., Taylor, J., Taylor, J.R.N., 2011. Effect of suppressing the synthesis of different kafirin sub-classes on grain endosperm texture, protein body structure and protein nutritional quality in improved sorghum lines. J. Cereal Sci. 54, 160 167, (da Silva et al., 2011). j From Naves, M.M.V., Castro, M.V.L., Mendonc¸a, A.L., Santos, G.G., Silva, M.S., 2011. Corn germ with pericarp in relation to whole corn: nutrient contents, food and protein efficiency, and protein digestibility-corrected amino acid score. Food Sci. Technol. 31 (1), 264 269, (Naves et al., 2011). k From Boye, J., Wijesinha-Bettoni, R., Burlingame, B., 2012. Protein quality evaluation twenty years after the introduction of the protein digestibility corrected amino acid score method. The Br. J. Nutr. 108, S183 S211, (Boye et al., 2012). l From Nitrayova´, S., Brestensky´, M., Heger, J., Patra´ˇs, P., 2014. Protein digestibility-corrected amino acid score and digestible indispensable amino acid score in rice, rye and barley. In: Proceedings of the XVII International Symposium, “Feed Technology”, October 25 27, 2016, Novi Sad, Serbia, pp. 90 95. ,https://www.cabdirect.org/cabdirect/abstract/20173322729. (accessed 09.11.018), (Nitrayova´ et al., 2014). b

SAA, sulfur amino acids (methionine 1 cysteine), AAA, aromatic amino acids (phenylalanine 1 tyrosine).

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TABLE 4.2 Reported Values for protein Content, Indispensable Amino Acids (IAA) profile, Amino Acid Score (AAS), Protein Digestibility Corrected Amino Acid Score (PDCAAS), and Digestible Indispensable Amino Acid Score (DIAAS) of Representative Proteins From Animal Origin Beefa

Chickenb

Fishc

Eggd

Milke

18.7f

21.4f

18.4f

12.6f

3.2f

Tryptophan

209f

250f

206f

167f

75f

Threonine

816f

904f

808f

556f

143f

Isoleucine

840f

1130f

849f

672f

165f

Leucine

1477f

1605f

1498f

1088f

265f

Lysine

1555f

1818f

1693f

914f

140f

SAA

687f

866f

744f

652f

58f

AAA

1357f

1571f

1342f

1181f

299f

Valine

909f

1061f

950f

859f

192f

Histidine

640f

664f

543f

309f

75f

AAS

144f

136f

148f

136f

85f

PDCAAS (%)

114h

92j

124j

118i

110k

DIAAS-(%)

112h

108k

100g

113k

114k

Protein (g/100 g) IAA (mg/100 g)

a

Trimmed retail cuts, separable lean and fat, all grades, raw. Chicken, broilers or fryers, meat only, raw (DIAAS determined in breasts). c Sea bass, mixed species, raw. PDCAAS was determined in canned in oil tuna. d Whole, raw, fresh. (DIAAS determined in hard-boiled eggs). e Whole, 3.25% milkfat. f From Nutrition Data. Available from: https://nutritiondata.self.com. g From Shaheen, N., Islam, S., Munmuna, S., Mohiduzzaman, Md., Longvah, T., 2016. Amino acid profiles and digestible indispensable amino acid scores of proteins from the prioritized key foods in Bangladesh. Food Chem. 213, 83 89, (Shaheen et al., 2016) (determined in Tilapia). h From Ertl, P., Knaus, W., Zollitsch, W., 2016. An approach to including protein quality when assessing the net contribution of livestock to human food supply. Animal 10 (11), 1883 1889, (Ertl et al., 2016). i From Schaafsma, G., 2000. The protein digestibility-corrected amino acid score. J. Nutr. 130 (7), 1865s 1867s, (Schaafsma, 2000). j From Boye, J., Wijesinha-Bettoni, R., Burlingame, B., 2012. Protein quality evaluation twenty years after the introduction of the protein digestibility corrected amino acid score method. The Br. J. Nutr. 108, S183 S211, (Boye et al., 2012). k From Marinangeli, C., House, J.D., 2017. Potential impact of the digestible indispensable amino acid score as a measure of protein quality on dietary regulations and health. Nutr. Rev. 75 (8), 658 667, (Marinangeli and House, 2017). SAA, sulfur amino acids (methionine 1 cysteine). AAA, aromatic amino acids (phenylalanine 1 tyrosine). b

representative proteins of animal and plant origin, in terms of the content of indispensable amino acids, chemical score, PDCAAS, and DIASS. Another important attribute of proteins is their contribution to physical properties of food systems due to their ability to form foams, gels, doughs, emulsions, and fibrous

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structures (Weder and Belitz, 2003). This set of capabilities, known as functional properties, provide to proteins the means to modulate texture, palatability, and, in general, the sensory properties of foods (Phillips et al., 1994; Aryee et al., 2018). There is a lot of literature dealing with the functional properties of proteins (Phillips and Williams, 2011; Lam and Nickerson, 2013; Soria-Herna´ndez et al., 2015; Li-Chan and Lacroix, 2018). A growing world population demands a wide variety of protein ingredients. The food and beverage, pharmaceutical, animal feeding, cosmetics, and personal care industries, are what drive this market, for which a value of US$58.49 billion is projected for the year 2022, with an annual growth rate of 6% from 2017 (Markets and Markets, 2017). Within this market, the segment with the highest projected growth is that of sports nutrition and functional beverages. The most demanded proteins are those of animal origin (GrandViewResearch, 2018). However, there are also consumer groups interested in health or environment subjects, who are demanding plant protein.

4.3 PLANT-BASED PROTEINS IN THE SUSTAINABILITY CONTEXT The population increase and the capacity to produce food is one of the most relevant current issues. It is not the amount of foods per se that matters most, because if these were distributed equally, the average global demand for nutrients could be met (Wood et al., 2018). What is really disturbing is the sustainability of their production. Although the concept of food sustainability is subject to many interpretations, the definition used in the statement from the World Commission on Environment and Development (Aiking and de Boer, 2004) can be adopted in a very appropriate way. In this statement, it is implicit that in order to feed an entire population, means must be used that do not have negative repercussions on the environment, and that do not compromise the natural resources of future generations. In this sense the current system of food production has a strong environmental impact (IOM and NRC, 2015) that must be reversed in the short term to avoid consequences of greater scope. In the context of mass food production, proteins are the focus of attention due to the essential biological functions that they perform (Moore and Soeters, 2015) and because for a long time it has been promoted that those of animal origin are of better quality. Thus, the greater purchasing power of the population encourages a greater consumption of proteins of animal origin (Sabate and Soret, 2014), which in turn drives the intensive production of poultry, livestock, and fish. A growing demand for animal protein has a high environmental cost. On the one hand, there is the greatest emission of greenhouse gases by livestock, contributing to global warming (Herrero et al., 2013). On the other hand, the inefficient conversion of vegetable protein to animal protein (Shepon et al., 2016) results in a high demand for animal feed, with large areas of land being allocated to monoculture of grains and causing indiscriminate deforestation, and depletion of aquifers (Rojas-Downing et al., 2017). The final effect is counterproductive because it contributes to the generation of desert areas of thousands of hectares, which leads to water scarcity, a reduction in food production and, therefore, in the migration of people to more hospitable areas with the

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FIGURE 4.1 Scheme that summarizes the series of events and impacts of an animal protein-based diets and the counterpart of shifting to a plant protein-based one. (Earth image credit: NASA).

subsequent social problems and potential risks related to public health (WHO, 2018). In Fig. 4.1 these impacts are condensed and schematized. This problem has aroused a real interest to reduce the consumption of animal protein, substituting the contribution of essential amino acids with the inclusion of plant protein. This chapter deals with proteins of plant origin that are of interest to academics and industrialists in the context of food sustainability. The objective is to provide information on nutritive aspects, extraction, and functional and bioactive properties of these proteins, in order to contribute to the formation of a criterion with scientific grounds on the factors to consider when their use is intended.

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4.4 PROPERTIES AND EXTRACTION OF PLANT PROTEINS Due to their low solubility in water, traditional methods of recovering plant protein include alkaline and alcoholic extraction, as well as isoelectric precipitation. The classical extraction presents some drawbacks, for example, low yields and using reagents or conditions that can damage biomolecules, in addition to the disposal or final handling of chemicals representing environmental risks. Thus, developing sustainable techniques for extracting plant proteins from conventional and unconventional sources is a current subject (Pojic et al., 2018). In the present chapter plant by-products are preferably discussed because their proteins are usually underutilized.

4.4.1 Cereal and Pseudocereal Proteins 4.4.1.1 Rice Bran Proteins With almost 759 million tons, in 2016 rice was the third most produced cereal in the world (FAOSTAT, 2016a). Rice is harvested as paddy rice, that is, the grains are enveloped by a husk, which is removed in the first step of a process called milling to give brown rice as product. In a subsequent step, the bran is removed to obtain white rice. Paddy rice milling yields 8% 12% of bran (Dapˇcevi´c-Hadnaðev et al., 2018) into which the rice proteins are concentrated (11.3% 14.9% by weight) (Schramm et al., 2007), and these are mainly storage proteins (Juliano, 1985), including albumins, globulins, prolamins, and glutelins (Fabian and Ju, 2011). Rice bran proteins have a true digestibility equal to casein (94.8%) and higher than proteins from rice endosperm (90.8%), soybean (91.7%), and whey (92.8%) (Han et al., 2015). Although the PDCAAS of rice bran proteins (90) is lower than casein (100) and soybean proteins (95) (Han et al., 2015) the rice bran stands as a good economic and nutritive source of protein. Rice bran is perhaps the most studied cereal by-product regarding the extraction and functional properties of proteins. This subject has been reviewed by several authors (Fabian and Ju, 2011; Phongthai et al., 2017; Al-Doury et al., 2018; Balandra´n-Quintana, 2018). Because of space limitations, here the state-of-the-art will be briefly addressed and updated. Alkaline extraction of rice bran proteins at pH 7 12 yields 30% 50% proteins and these values are raised to more than 90% if extraction is done with combinations of solvents (Fabian and Ju, 2011). Optimal conditions for the alkaline extraction of defatted rice bran have been reported at pH 10, 80 rpm and 300 minutes of stirring, 52 C, with an extraction yield of 34.51% and protein content in concentrates of 48.53% (Bernardi et al., 2018). Ultrasound-assisted water extraction of defatted rice bran results in an increased yield of protein and improves the rate of initial extraction up to 3.5-fold (Ly et al., 2018). Water and oil absorption capacity, emulsifying capacity, and emulsion stability are not affected by ultrasound, whereas increased gelation capacity and minor foaming capacity and stability were reported (Ly et al., 2018). On the other hand, ultrasound power affects significantly the total phenolic content, metal chelating activity, and antioxidant (radical scavenging) activity of rice bran proteins (Iscimen and Hayta, 2018).

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Functional properties of rice bran proteins depend on the rice cultivar and this is related to different proportions of the secondary structure of proteins between cultivars, that is, β-sheets, α-helix, or β-turns (Singh and Sogi, 2018). Another important factor to take into account is the high lipase activity of rice bran, which makes a stabilization treatment mandatory to prevent rancidity. Such a treatment must not be deleterious to functional properties or result in significant low protein yields. The advice is to monitor the effect of the stabilizing treatment on the properties of interest in order to take the best decision. For example, microwave and dry heating as stabilizing treatments cause a decrease in protein yield but a higher purity, whereas the oil absorption and the emulsifying capacity are improved, and water holding and foaming properties are slightly impaired (Lv et al., 2018). There are a lot of bioactive properties reported for rice bran proteins or their hydrolysates. Because of their high selectivity to polyphenols of high antioxidant capacity, such as the tea catechins, rice bran proteins have been proposed as a matrix to deliver catechins to gastrointestinal tract (Shi et al., 2017). Also, rice bran proteins are considered as nutraceuticals to improve the cholesterol metabolism (Wang et al., 2017a). On the other hand, hydrolysates of rice bran proteins have shown a series of activities, such as antimicrobial (Taniguchi et al., 2017), inhibition of angiotensin-I converting enzyme and glucosidase (Pooja et al., 2017; Wang et al., 2017b; Uraipong and Zhao, 2018), antioxidant activity (Moritani et al., 2017; Phongthai et al., 2018), reduction of arterial stiffening caused by metabolic syndrome (Senaphan et al., 2018), and attenuation of diabetic nephropathy (Boonloh et al., 2018). All of these reports suggest a great potential for rice bran proteins as supplements or functional foods. 4.4.1.2 Wheat Bran Proteins Wheat (Triticum aestivum L.) is the second most important cereal cultivated worldwide with 740 million tons produced in 2016 (FAOSTAT, 2016a). Wheat bran consists of a series of layers that surrounds the wheat grain and which are obtained as a flaked by-product during milling, whereas flour is the main product. Wheat bran has 12% 2 19% proteins. As bran represents 15% of the grain weight, and because it is mainly intended for animal feed, there are many million tons of proteins that are wasted or underutilized each year. The latter is important because wheat bran proteins are of better quality than those of flour due to their AAS and digestibility. For many years attempts have been made to take advantage of wheat bran proteins, however, to the best of our knowledge there are no extensive uses for them, probably due to drawbacks in extraction and low yields. Nevertheless, new approaches and modifications to classical extraction methods in order to make them more sustainable and improve protein yields are frequently proposed. Updated reviews on this subject have been performed (Balandran-Quintana et al., 2015; Balandra´n-Quintana, 2018; Balandra´n-Quintana and Mendoza-Wilson, 2018), so it will not be addressed in detail here. 4.4.1.3 Sorghum Proteins Sorghum is the fifth most important cereal in the world, after corn, wheat, rice, and barley (Awika and Rooney, 2004). World production of sorghum for the period 2017 2 18 reached 59.24 million metric tons, concentrated in the United States, Nigeria, Me´xico,

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India, Ethiopia, Sudan, China, Argentina, and Australia (USDA, 2018). Around 35% of the sorghum produced is intended for human consumption (porridges, sausages, pasta, cookies, tortillas, bread, snacks, alcoholic, and nonalcoholic beverages), the rest is used for animal feed and industrial applications, mainly bioethanol production (Awika and Rooney, 2004; Dicko et al., 2006; Tuinstra, 2008). On average, the whole grain of sorghum is constituted of 65% 2 80% of carbohydrates, 3.5% 2 18% proteins, 1.5% 2 6% lipids, 1% 2 4% ash, and 8% 2 12% moisture (Lasztity, 1996; Dicko et al., 2006; Badigannavar et al., 2016). Within the components of sorghum, the presence of fiber and tannins is highlighted (2% and 7% 2 8%, respectively), due to their impact on the digestibility of proteins and amino acid availability in the grain (Deshpande et al., 1986; Kulamarva et al., 2009). Sorghum proteins are classified in kafirins (prolamins), glutelins, albumins, and globulins. Kafirins make up 50% 82% of storage proteins located in the endosperm. Based on their molecular weight (MW) kafirins are divided into four groups: α, β, γ, and δ. α-Kafirins represent approximately 80% of total kafirins and include polypeptides with molecular weights of 23 and 25 kDa; β-kafirins (16, 18, and 20 kDa MW) range 8% 2 13%; γ-kafirins (20 2 28 kDa) content fluctuates between 9% and 21%; and δ-kafirins have a MW about 13 kDa and are present in very low amounts (Belton et al., 2006; Dicko et al., 2006; De Mesa-Stonestreet et al., 2010). In general, kafirins are distinguished by their high content of glutamic acid, proline, leucine, and alanine, but have reduced amounts of essential amino acids, such as lysine, threonine, tryptophan, and total sulfur amino acids (De MesaStonestreet et al., 2010). Glutelins are storage proteins located mainly in the endosperm, where they constitute around 16% 2 35%. Unlike kafirins, glutamic acid content in glutelins is low, but their contribution of the essential amino acid lysine is high (Taylor and Schu¨ssler, 1986; Holding, 2014). Albumins and globulins are storage proteins that abound in the germ with values of 32% 2 35%, MW of 75 2 100 kDa and 30 kDa, respectively, and are rich in essential amino acids, especially lysine (Haikerwal and Mathieson, 1971; Taylor and Schu¨ssler, 1986). Protein digestibility among sorghum varieties is highly variable; through in vitro and in vivo studies, values have been reported ranging from 30% to 70% (IAEA, 1977). Sorghum grain proteins have a significantly lower protein digestibility compared to other cereals (corn and wheat). The low digestibility of sorghum is attributed to the interaction of its proteins with tannins and fiber, which act as antinutritional factors (Badigannavar et al., 2016). Likewise, reduced solubility of kafirins and an increase in resistance of these to be digested by proteases such as pepsin has been observed when sorghum is cooked, which limits the use of sorghum grain as a primary source of protein (Anglani, 1998). In order to solve the problems of digestibility of sorghum proteins, high lysine sorghum genotypes have been developed, which have an enormous potential to be used as a food source of essential amino acids. These genotypes are distinguished from the main varieties of cultivated sorghum by having low values of kafirins (0.62 and 0.35 mg/g grain DW of α- and β-kafirins, respectively) and intermediate levels of glutelins (12.47 mg/g grain DW), albumins, (3.88 mg/g grain DW), and globulins (0.73 mg/g grain DW). Additionally, large variability in MW of proteins has been detected: α-kafirins 14 2 89 kDa, β-kafirins 16 2 56 kDa, glutelins 21 2 84 kDa, albumins 19 2 87 kDa, and globulins 15 2 64 kDa (Vendemiatti et al., 2008).

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Traditionally, differential solubility extraction methods have been used for the isolation of sorghum proteins. Following a sequential procedure, albumins and globulins are extracted with water and sodium chloride solution; kafirins with 60% tert-butanol and 2mercaptoethanol, and glutelins with alkali borate and sodium dodecyl sulfate, achieving a recovery of 26% 2 40% (Youssef, 1998; De Mesa-Stonestreet et al., 2010). However, other methods have been implemented with the purpose of improving extraction time, percentages of recovery, purity, digestibility, and functionality of the proteins, as well as the recovery of industrial by-products proteins. In this sense the addition of detergents and suitable reducing agents for food analysis have been proved to modify both the digestibility and extractability of sorghum proteins. The extraction of sorghum proteins with a 12.5 mM sodium borate buffer, pH 10.0, containing 2% of sodium dodecyl sulfate and 2% β-mercaptoethanol, using a 20:1 solvent-to-sample ratio (v/w) and three extraction intervals of 5 minutes, allows to isolate 84% of proteins reducing the time of extraction up to 80% (Park and Bean, 2003). On the other hand, treating decorticated sorghum flour with thermostable α-amylase employing extruder or batch mixer, allows to separate proteins and starch by a faster process that yields concentrates with higher protein contents (up to 80%) and more digestible proteins (De Mesa-Stonestreet et al., 2009). Sonication has also been used to make more efficient the extraction of sorghum proteins, separating them rapidly from the starch. Extracting protein from whole ground sorghum flour with 70% ethanol for 1 hour at 50 C followed by 4 minutes of sonication, increases the purity of proteins from 31% 2 52% up to 78% (Bean et al., 2006). The benefits of extraction by sonication have been remarkable and are achieved by modifying the secondary structure of kafirins, increasing their solubility, and improving their antioxidant and anti-inflammatory abilities (Cullen, 2017). The extraction of kafirins from sorghum distillers dried grains with solubles (by-product in bioethanol production), using acetic acid as solvent instead of traditional alcohols, yields 44.2% of kafirins with the highest purity (98.9%) (Wang et al., 2009). Sorghum proteins have low functionality because of their poor rheological properties with regard to cohesivity, pliability, extensibility, and rollability (Kulamarva et al., 2009; Espinosa-Ramı´rez et al., 2017). To solve the problems of sorghum protein functionality, several efforts have been performed, among these the search for efficient food-grade extraction methods (chemical, enzymatic) to isolate functional proteins, as well as the genetic manipulation to develop improved sorghum varieties. One of the chemical methods that have been developed to improve the functional properties of sorghum proteins consists of their conjugation with dextran or galactomannan. The sorghum proteins are extracted in an aqueous alkaline (pH 8) medium containing 2-mercaptoethanol, then are mixed with dextran or galactomannan at a ratio 1:5 and then freeze-dried. Both sorghum protein and conjugates increase their water solubility up to 90% 2 95% and their emulsifying capacity up to twice that of sorghum protein alone (Babiker and Kato, 1998). Regarding enzymatic methods, kafirins extracted from decorticated sorghum flour using 70% aqueous ethanol and sodium meta-bisulfite at 65 C, and subsequently treated with a protease, show higher protein purity (95%), improved protein digestibility (89%), better water holding (2.8 vs 1.9 g/g), and higher fat absorption capacities (2.4 vs 1.6 g/g) compared to extracts from ground decorticated sorghum (EspinosaRamı´rez et al., 2017). A flour obtained from a variety of genetically improved sorghum,

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which is characterized by having proteins with high digestibility and high lysine content, has shown significantly improved extensibility properties compared to normal sorghum varieties (Goodall et al., 2012). Although sorghum proteins have low digestibility and functionality, their potential as bioactive molecules is important. Kafirins have been shown to be useful in the inhibition and downregulation of expression of signal molecules generating inflammatory response (Holding, 2014). Such bioactive effect is enhanced when kafirins are extracted by means of sonication, since it alters the secondary structure of these proteins, increasing their solubility and ability to halt the production of proinflammatory cytokines through inhibition of reactive oxygen species in THP-1 human macrophages. 50 2 100 μg kafirin/mL are enough to induce these effects (Cullen, 2017). One hydrolysate rich in peptides of α-kafirinin, obtained with 40 μg chymotrypsin/mg α-kafirin, was able to inhibit in vitro the angiotensin-I converting enzyme, which suggests it may be useful in treating high blood pressure (Kamath et al., 2007). Peptides generated from kafirin in vivo hydrolysis in rats fed with diets supplemented with sorghum kafirin extract, induced a decrease in the levels of total cholesterol, and increased the serum antioxidant potential as well as the low density lipoprotein cholesterol levels, suggesting a role for kafirins to reduce the risk of cardiovascular diseases (Ortı´z-Cruz et al., 2015). Enzymatic deamidation, used to improve solubility, emulsification, stability, and foaming of cereal storage proteins, is a food-compatible method that has not been tested in sorghum proteins and which could be advantageous for the exploitation of these proteins. Likewise, in vitro and in vivo studies of the bioactive properties of sorghum proteins have been limited by their digestibility drawbacks. Both issues represent an area of opportunity to generate relevant research for future applications of sorghum proteins. 4.4.1.4 Barley Proteins Barley is the fourth largest cereal in the world (FAOSTAT, 2016a). On a dry basis, carbohydrates predominate (78% 83%) its chemical composition, among which starch (60% 65%), arabinoxylans (4.4% 7.8%), β-glucans (3.6% 6.1%), and cellulose (1.4% 5%) are found in the largest proportions. Proteins are second (8% 15%), while lipids (2% 3%), minerals (2% 3%), and others, including B vitamins, are minor components (Izydorczyk et al., 2014). About 75% of the cultivated barley is used as forage. Most of the remaining 25% is directed to produce alcoholic beverages, mainly beer, while a small proportion is processed to obtain β-glucans or consumed directly by humans. Protein content of barley grain is cultivar-dependent (Yu et al., 2017). These proteins have nutritional and functional properties that could compete with those of soybean (Houde et al., 2018). Barley flour proteins are extracted by different methods. For the classical alkaline extraction and isoelectric precipitation, different results are reported. For example, Alu’datt et al. (2012) obtained concentrates with 32.9% protein and 60.15% extraction yield, while Mohamed et al. (2007) reported concentrates with 90.5% protein content and 70% yield. On the other hand, Houde et al. (2018) reported yields of 51.4% with protein content of 68.9%. Isoelectric precipitation after alkaline extraction is beneficial, because although the yield is lower (57.1% vs 51.4%) the purity increases (33% vs 68.9%) due to selective isolation of the rest of the components. In order to increase yield and/or purity, other methods have been assayed. The use of amylase and amyloglucosidase to hydrolyze

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carbohydrates resulted in a protein recovery of 25.7% and, if a step of digestion with β-glucanase is included, this increases to 71.6% but the protein content decreases from 49% to 37%. If isoelectric precipitation is added to the tri-enzymatic treatment, the protein content and recovery increase to 41.4% and 78%, respectively (Houde et al., 2018). According to results, if purity is sacrificed the tri-enzymatic treatment could be a good alternative to alkaline extraction and isoelectric precipitation, since the recovery is higher. Economic factors of the process deserve a separate consideration. When barley is processed to produce beer, large amounts of brewers’ spent grain (BSG) are produced. BSG is a solid residue that remains from the must, having relatively highprotein content because this is concentrated as most of the starch is removed during the mash and used in fermentation (Negi and Naik, 2017). The protein content of the BSG is between 14.2% and 24.7% (Lynch et al., 2016), which are mostly storage proteins, that is, hordeins and globulins (Bi et al., 2018). BSG is generally used in animal feed (Ikram et al., 2017) or sent to landfills, so the proteins are wasted or underutilized and there is a growing interest in their recovery and use. Extraction of BSG proteins has been recently reviewed (Ikram et al., 2017; Balandra´nQuintana, 2018). Alkaline extraction and further isoelectric precipitation (Connolly et al., 2014) are usual methods, through which proteins can be recovered up to 85% (Vieira et al., 2014). Sequential extraction with salt and isopropanol, and further isoelectric precipitation, are reported to obtain the nonprolamin and prolamin fractions, respectively, of defatted BSG (50% wheat, 50% barley) (Negi and Naik, 2017). Combining solvent extraction with physical methods, e.g., pressing followed by sifting in the presence of water; sifting, with different combinations of solvents; wet milling, and ultrafiltration, are also reported. Concentrates with no more than 60% proteins have been obtained in most of these methods, except the alkaline extraction. Treatments prior to alkaline extraction and acid precipitation, e.g., steam explosion and proteolysis, can improve extraction yields. Proteolysis increases the solubility of proteins from 15% (untreated BSG) to almost 100%. Steam explosion reduces the enzymatic solubility of proteins, but allows a greater recovery during a subsequent centrifugation step. The drawback of these preextraction methods is the coextraction of lignin (Rommi et al., 2018). A nonconventional method is the extraction with deep eutectic solvents, for example using sodium acetate:urea in a 1:2 molar ratio, which permits to obtain concentrates with 50% protein and extraction yields up to 79%, due to dissolution of proteins which are insoluble by nature or that are denatured during the malting process (Wahlstrom et al., 2017). Regarding functional properties, alkali-extracted BSG proteins are poorly soluble in water, which affects other properties such as the capacity of emulsification and foam formation. Water solubility and therefore functional properties of BSG proteins can be improved by partial hydrolysis with proteases (Celus et al., 2007; Treimo et al., 2008; Yalc¸ın et al., 2008) and/or carbohydrases (Niemi et al., 2013) prior to extraction. Barley flour glutelins have higher oil absorption capacity and greater emulsion stability than hordeins, which in turn have a good foam capacity (Wang et al., 2010). In the nonprolamin fraction of wheat barley BSG, emulsion stability is 80% up to 110 minutes, whereas in the prolamin fraction it decreased, reaching 40% at 90 minutes. This behavior is due to a more balanced proportion of hydrophobic and hydrophilic amino acids in the nonprolamin fraction, according to authors (Negi and Naik, 2017). In this fraction, both the emulsion

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activity index and stability were higher at pH 9. The results suggest that the nonprolamin fraction of the wheat and barley BSG may have applications as emulsifier in the food industry (Negi and Naik, 2017). BSG proteins and some of their peptides produced by enzymatic hydrolysis can act as immunomodulators (McCarthy et al., 2013; Crowley et al., 2015) and possess antithrombotic activity (Cian et al., 2018). Hydrolysates of BSG (,10 kDa) released by different proteases also exert protective effects against toxicity by free radicals in Caco-2 and HepG2 cell lines; the effect depends on the protease used (Vieira et al., 2017). The presence of a peptide with dual inhibitory activity against angiotensin-I converting enzyme and DPP-IV has been found in BSG after enzymatic hydrolysis (Connolly et al., 2017). DPP-IV is an aminopeptidase that rapidly degrades the incretin hormones, which potentiate insulin secretion stimulated by glucose, so the inhibition of DPP-IV is one of the approaches used for the management of Type 2 diabetes (Connolly et al., 2017). On the other hand the angiotensin-I converting enzyme is key in the regulation of blood pressure and the target of inhibitory drugs that are prescribed to patients with hypertension (Daskaya-Dikmen et al., 2017). 4.4.1.5 Quinoa Proteins Quinoa (Chenopodium quinoa, Willd.) is not a true grain but a pseudocereal native to the Andes (Valencia-Chamorro, 2009). Its cultivation has also been introduced into Africa, Asia, Australia, Europe, and North America because of its great ability to adapt to different agro-ecological conditions (Valencia-Chamorro, 2016). Outside of South America the volumes of cultivated quinoa still do not seem to be very important. In 2016 148,720 tons of quinoa were produced in the world, distributed among only three countries: Peru, 53% of total; Bolivia, 44%; and Ecuador, 3% (FAOSTAT, 2016a). Quinoa is considered a complete food due to the quantity and quality of its proteins, as well as its content of vitamins, minerals, phytosterols, flavonoids, omega-6, and vitamin E (Abugoch, 2009; Vega-Galvez et al., 2010). Quinoa is recognized as “one of the grains of the 21st Century” (Vilcacundo and Herna´ndez-Ledesma, 2017) and 2013 was designated by FAO as “The International Year of Quinoa” (Valencia-Chamorro, 2016). There is extensive literature on the composition and nutritive, functional, and nutraceutical properties of quinoa (Lamothe et al., 2015; Tang et al., 2015; Navruz-Varli and Sanlier, 2016; Vilcacundo and Herna´ndez-Ledesma, 2017; Pellegrini et al., 2018). The outer layer or pericarp of quinoa grains contains between 2% and 5% of saponins (Medina-Meza et al., 2016; Woldemichael and Wink, 2001). Although saponins do not affect the nutritional quality of quinoa proteins (Ruales and Nair, 1992), they provide bitter flavors and are considered antinutrients that can damage the mucous membranes of the small intestine (Gee et al., 1993). Processing reduces both concentration and membranolytic activity of saponins (Gee et al., 1993) but it is recommended to remove them from grains before consumption (Medina-Meza et al., 2016). The latter can be achieved by water washing (Repo-Carrasco-Valencia and Serna, 2011). In addition, production of saponins in quinoa can be regulated by controlling the cultivation conditions, for example, saline stress and drought decrease the content of saponins in the grain by 50% and 45%, respectively (Go´mez-Caravaca et al., 2012).

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Protein content of quinoa is between 13.7 and 16.7 g/100 g of edible material, being higher than cereals such as rice, barley, corn, and rye (reviewed by Filho et al., 2017). The largest storage proteins are albumins and globulins, while prolamins are found in very low concentrations (Prakash and Pal, 1998; Abugoch et al., 2008; Vilcacundo and Herna´ndez-Ledesma, 2017). The latter is relevant since quinoa has potential as an ingredient in the manufacture of gluten-free products (Alvarez-Jubete et al., 2010; Jan et al., 2018; Kurek et al., 2018). Quinoa storage proteins are separated by SDS PAGE into four groups (Abugoch et al., 2008). The group with the highest molecular mass (  60 kDa) corresponds to type 11S storage proteins, named collectively as Chenopodina (Brinegar and Goundan, 1993). Chenopodina, in turn, consists of a basic and an acid subunit, with masses in the ranges 22 23 and 32 39 kDa, respectively (Brinegar and Goundan, 1993; Brinegar et al., 1996). Finally, peptides with molecular mass ,20 kDa are identified as albumins (Abugoch et al., 2008; Toapanta et al., 2016), among which a fraction of 8 9 kDa has been characterized as type 2S (Brinegar et al., 1996). The latter is interesting because of its high content of arginine and histidine, amino acids that are essential for children (Brinegar et al., 1996). Proteins of quinoa seeds have an AAS higher than cereals (Ruales and Nair, 1992). The content of lysine in the quinoa grains is relatively high since this amino acid is not very abundant in plant proteins (Table 4.1). The in vitro protein digestibility of raw quinoa fluctuates between 76% and 78%, being lower than that of proteins of animal origin but very similar to that of other plant proteins (Lo´pez et al., 2018). The protein efficiency ratio (PER) of raw quinoa seeds devoid of saponins is between 78% and 93% relative to casein, and increases to 102% 105% when the seeds are cooked. Alkaline extraction and subsequent acid precipitation is the best method for obtaining quinoa protein isolates; the higher the extraction pH, the greater the amount of recovered protein (Abugoch et al., 2008; Elsohaimy et al., 2015; Navarro-Lisboa et al., 2017). Isolates with 77% and 83% (w/w) of protein have been reported at extraction pH of 9 and 11, respectively (Abugoch et al., 2008). However, if the pH is too alkaline it could affect the water solubility of proteins due to denaturation and formation of agglomerates, since average solubility of 30% has been reported when the extraction is done at pH 11, versus 75% 98% when extracting at pH 9; in both cases the solubility has been measured in a pH range of 3 11 (Abugoch et al., 2008). On the other hand, the extraction pH in the alkaline range (9 11) does not significantly affect the content of essential amino acids or other functional properties, such as the water absorption capacity, which is around 4 mL H2O/g protein, a value very similar to that of soy protein isolates (4.3 mL H2O/g protein) (Abugoch et al., 2008; Elsohaimy et al., 2015). The oil absorption capacity of quinoa proteins (extraction at pH 10 and precipitation at pH 4.5) is 1.88 mL/g, close to 2.1 which is the value reported for soybeans. The foaming capacity is lower than the average value for egg white albumin, which is used as a reference (69.28% vs 178%). However, in terms of foam stability, reported values are very similar for both proteins (around 54%) (Elsohaimy et al., 2015). The average emulsification capacity index of quinoa proteins is 2.1 m2/g calculated within a range of protein concentration from 0.1% to 3%, at pH 10. At the same conditions, the stability of the emulsion is 38.4 minutes on average (Elsohaimy et al., 2015). Aluko and Monu (2003) reported emulsification capacity indexes of almost 50 m2/g for a protein concentration of 1% (w/v), pH 8, which is a huge

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difference since in both studies the same method was used. In the latter case, the stability of the emulsion was almost 100% after 30 minutes (Aluko and Monu, 2003). Although quinoa is a promising food, it is necessary to systematize its production, as well as to make protein extraction methods more efficient in order to make it a sustainable process (Scanlin and Lewis, 2017).

4.4.2 Proteins from By-Products of Plant Oil Refining Industry 4.4.2.1 Soybean Proteins Soybean (Glycine max L. Merr.) is an annual legume plant (Leguminosae or Fabaceae family) native to East Asia, widely grown in America, China, and India, and consumed worldwide as a cooking oil, animal feed or food ingredient (FAOSTAT, 2016a). Soybean seeds are rich in oil (15% 25%), protein (35% 45%), and carbohydrate (33%, insoluble and soluble) contents. Seed composition can be affected by genetic and environmental factors (Zarkadas et al., 2007). Salt-soluble globulin proteins glycinin (300 380 kDa, 11S), and β-conglycinin (150 200 kDa, 7S) are the major dominant storage proteins (65 85%) in soybean seed. Other minor proteins (2% 5% of the total seed proteins) include β-amylases, Kunitz trypsin inhibitor (20 25 kDa), Bowman Birk inhibitor (8 kDa), chymotrypsin inhibitor, urease, lipoxygenases, and soybean lectins (120 kDa, 7S) (Fukushima, 2011). Oleosins account for 8% 20% of seed proteins (Murphy, 2008). Methionine and cysteine are the most nutritional limiting amino acids of soybean proteins. However, soybean proteins have a PDCAAS of 90 99 indicating that they provide a good balance in amino acid composition for human consumption (Young, 1991; Fukushima, 2011). Defatted soybean flakes, a by-product remaining after oil extraction, is the major source of commercial soybean proteins. A less usual extraction process uses the whole seed to obtain a soy-base (a water extract of dehulled soybeans) from which soy milk, tofu, and soy fruit beverages are produced (Preece et al., 2017b). Before being processed into soybean meal, ground defatted soybean flakes receive a desolventizing-toasting process in order to remove residual hexane and to inactivate antinutritional factors like lectins and protease inhibitors. The resulting soybean meal is mainly used as a protein source in animal feed (Fukushima, 2011). Soy protein products for human consumption are obtained from soybean meal. These include soy flour (with a finer particle size than soybean meal, 56 59% protein); soy protein concentrates (65% 72% protein); soy protein isolates ($90% protein); and texturized soy proteins. To process soybean meal in food products it is necessary to minimize protein denaturation in order to obtain high water soluble proteins. This is achieved by replacing the desolventizing-toasting process for a superheated hexane vapor process. Commercial production of this process is discussed in detail by Liu (1997). Soy flour is obtained by grinding the soybean meal to make a powder whose particles pass through a 100-mesh screen. Soy protein concentrates are prepared by removing soluble carbohydrates from soy flour. This can be achieved by protein denaturation using aqueous ethanol (50% 80%) extraction; by attaining the protein isoelectric point (pH 4.5); or by a moist heat treatment. After separation by centrifugation, the proteins are dispersed in water and spray-dried to produce the soy concentrates (Fukushima, 2011).

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For soy protein isolates production, both soluble and insoluble carbohydrates are removed. In the commercial processes, proteins and soluble carbohydrates are first extracted using water or a mild alkali extraction (pH 7 10). The precipitate (mostly insoluble carbohydrates) is separated by centrifugation. Then, the protein is precipitated by isoelectric point, resuspended in water and spray dried (Preece et al., 2017b). Other methods developed to produce SPI include the conventional extraction followed by ultrafiltration and diafiltration; alkali extraction followed by ultrafiltration reverse osmosis and diafiltration. These membrane processes yield more soluble proteins because of the exclusion of the acid precipitation step (Liu, 1997). For research purposes, the protein extraction methodology depends mainly on the research objective. For example, glycated proteins were usefully extracted using a solution which contained phosphate buffer, sodium metabisulfite, ascorbic acid, and sodium chloride (Serra et al., 2016) using enzyme-assisted microwave followed by ultrasound- and cavitation-assisted extraction (Wang et al., 2014; Lu et al., 2016; Preece et al., 2017a). These and other extraction processes were discussed in detail by Luthria et al. (2018). Off-flavors and allergenic proteins are two main factors, which limit the expansion of soy protein consumption in western countries. Off-flavors are produced by lipoxygenases (beany, grassy flavors), isoflavones, and saponins (bitter, astringent, chalky flavors). Despite many studies, a process that removes or mask these components satisfactorily has not been developed (Fukushima, 2011). There are at least 18 soybean proteins considered as potential allergens (Gly m 1 to Gly m 8; Gly m BD 28 K and 30 K; lipoxygenase; soybean hemagglutinin, among others). However, data on a single potential soybean allergen protein is difficult to obtain because clinical reactivity analysis uses crude soybean extract or soybean formulas to evaluate allergenicity (Selb et al., 2017). Soybean allergy worldwide prevalence is 10-fold less common in adults (0.27% prevalence) than in children (Katz et al., 2014). It is not possible to remove the soybean allergens with the current methodology. However, some research showed that application of high-intensity ultrasound, microwave, high-pressure homogenization, and high hydrostatic pressure reduced SPI allergenicity by approximately 19%, 25%, 30%, and 47%, respectively (Li et al., 2016). In addition to their nutritional value, soybean proteins have an important role in food functionality. Because of their gelling/textural capabilities, fat and water absorption, and emulsifying properties they are recognized worldwide as versatile ingredients with great consumer acceptability. 4.4.2.2 Rapeseed/Canola (R/C) Proteins Rapeseed (Brassica napus L. spp oleifera) is the second largest oilseed crop in the world cultivated mainly in the colder temperate regions of Canada, China, Australia, Europe, and India (FAOSTAT, 2016b). A group of rapeseed varieties with special characteristics (,2% of erucic acid in oil and ,30 μM of glucosinolates in its solid content) was registered as canola by Western Canadian Oilseed Association in 1978 (Wanasundara et al., 2017). Cruciferin (salt-soluble globulin, 230 300 kDa) and napin (water soluble albumin, 12 14.5 kDa) are the two major proteins of R/C. They account for 65% and 25% of total R/C seed proteins, respectively (Perera et al., 2016). Napin may cause allergic symptoms in hypersensitive individuals (Palomares et al., 2002). Other minor proteins are the oil body proteins oleosins (B18 kDa) and caleosins (27 kDa) (Jolivet et al., 2009). R/C protein

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fractions can be separated by electrophoresis, anion exchange chromatography, membrane filtration, and ultrafiltration (Aider and Barbana, 2011). The amino acid composition of R/C proteins is highly influenced by the method of protein extraction (Wanasundara et al., 2017). For example, alkaline extraction produces protein with lower levels of lysine which might be due to the formation of lysinoalanine (Shahidi et al., 1992). In general, R/C proteins have high contents of arginine, glutamic acid, glutamine, and isoleucine and leucine, and low amounts of methionine and cysteine. Lysine is the first limiting amino acid followed by valine (Ivanova et al., 2016). R/C meal, a by-product remained after oil extraction, is the major source of R/C proteins (B50% of meal dwt). Other R/C meal compounds are carbohydrates (B20%) and some antinutritional factors, such as phenolics (tannins and sinapine), glucosinolates (3-butenyl glucosinolate, 4-pentenyl glucosinolate, 2-hydroxy-3- butenyl glucosinolate, and 2-hydroxy-4-pentenyl glucosinolates), and phytates (Wanasundara et al., 2017). These antinutritional factors limit the use of R/C proteins in food applications. Commercial R/C meal is mainly used as animal feed in aquaculture and livestock industries. However, concentrations of some of these compounds can be diminished by developing special rapeseed cultivars using genetic selection tools or through chemical modifications, membrane filtration, or microbial treatments (Aider and Barbana, 2011). Thus the development of innovative technologies could allow the use of R/C proteins for human consumption. The most common procedure to concentrate or isolate R/C proteins (obtained 30% of initial meal protein content) is based on aqueous extraction in the presence of alkali (pH, near neutrality) followed by acidic precipitation (Aider and Barbana, 2011). However, higher pH is needed to increase protein recuperation, allowing phenols and phytates extraction and delaying salt elimination (Perera et al., 2016). Normally, alkaline extraction yields low solubility proteins with dark colors because of the dramatic change of pH during extraction and also the formation of protein polyphenol interactions and/or polyphenol oxidation (Wanasundara et al., 2017). The addition of sodium bisulfite or sodium metaphosphate may produce less discolored protein isolates (Mahajan and Dua, 1994). Ghodsvali et al. (2005) implemented a three-step procedure for R/C protein isolation. After alkali extraction and acidic precipitation, an ultrafiltration (10 kDa) step was implemented, followed by diafiltration and drying. The obtained isolate was high in protein content (90%) and low in glucosinolates (2 μM) and phytates (1%). Diosday et al. (1984) obtained a protein isolate (89% protein content) free of glucosinolates through aqueous extraction followed by ultrafiltration. A solvent-free oil extraction by cell wall enzymatic degradation and/or cold-press followed by flash chromatography produced a 40% 50% protein-enriched meal (Wanasundara et al., 2017). Other alternative technologies such as enzyme-assisted wet fractionation and dry fractionation have been studied in order to save water and energy consumption. Fractionation during recovery optimizes biological, chemical, and technological functionality of R/C proteins. For example, the formation of a protein micelle mass (PMM) by protein salting-in followed by hydrophobic aggregation promotes the obtaining of a cruciferin-rich fraction and a napin-rich fraction (Burcon Nutrascience MB Corp 2008). Expanded bed absorption-ion exchange chromatography (EBA-IEC) was used by Pudel et al. (2015) for the scale-up isolation of napin (98%) and cruciferin (95%).

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Functional properties of R/C proteins largely depend on the protein composition, type of processing, and protein-associated components (Wanasundara et al., 2017). In general, isolates prepared from alkaline extraction possess unacceptable water-holding capacity and poor emulsification and poor foaming capacities (Aider and Barbana, 2011). Protein chemical modification, including acetylation, succinylation, glycation, and enzymatic hydrolysis have been conducted in order to improve these functional properties (Gruener and Ismond, 1997; Alashi et al., 2014; Pirestani et al., 2017). Potential uses of R/C protein peptides with bioactive activity have been reported. Bioactivity includes mainly antihypertensive (He et al., 2013a) and antioxidant (Alashi et al., 2014). Akbari and Wu (2015) reported the synthesis of chitosan cruciferin nanoparticles for carotene delivery while Hong et al. (2017) studied the role of amphipathic peptides in the obtaining of cruciferin nanoparticles by cold gelation. All these methodologies need the development of scale-up and competitive technologies in order to incorporate R/C protein products in human food (Wanasundara et al., 2017). 4.4.2.3 Cotton Proteins Cotton (Gossypium hirsutum L.) is the third largest oilseed crop in the world and also a source of relatively high-quality protein (Campbell et al., 2014). Globulins (salt soluble, vicilin, and legumin families) are the major dominant storage proteins in cottonseed and account for 60% 70% of seed proteins. Albumins (water soluble) and gliadins (alkali soluble) are in low concentrations (Bellaloui et al., 2015). The most abundant amino acid is arginine (15% 34% of total protein) while methionine and cysteine are the least abundant (1% 2%) (He et al., 2015). Cottonseed meal (CM), a by-product remained after oil extraction, is the major source of commercial cottonseed proteins. CM is of two types depending on oil extraction, solvent extraction (more common) and expeller extraction. Both meals contain 33% 41 % of protein and also a harmful terpenoid derived from (1)-δ-cardinine named gossypol which is cardio- and hepatotoxic for humans and other monogastric animals (Gadelha et al., 2014). Part of gossypol present in the CM binds to the proteins forming Schiff bases with lysine (Pelitire et al., 2014). Because of this, raw cottonseed proteins (CM) are mainly used as fertilizer and as a protein supplement for ruminant animals which possess a detoxifying system for gossypol (Campbell et al., 2014). Nonfood potential protein products include bioplastics and films (Yue et al., 2012) and bio-based wood adhesives (Cheng et al., 2016). In 2014 17 the global production of cottonseed was about 39 44 million metric tons/ year, which means between 8.3 and 9.4 million metric tons of available protein. Options to produce free gossypol cottonseed include the transfer of gossypol glandless mutant into commercial cultivars and the use of RNA interference (RNAi) technology. Sunilkumar et al. (2006) used tissue-specific RNAi mediate suppression to disrupt the synthesis of gossypol to develop transgenic seeds with 99% reduction of gossypol content. Richardson et al. (2016) used meal from these transgenic seeds as feed ingredient for shrimps without toxic effect. Pelitire et al. (2014) explored the gossypol extraction from cottonseed proteins using ethanol-based solutions in the presence of phosphoric acid to promote the hydrolysis of protein-bound gossypol. However, the toxic compound reduction was only 5% 10%.

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Cottonseed protein isolates can be prepared from defatted CM by alkaline protein solubilization followed by isoelectric precipitation (Zhang et al., 2009). Optimized extraction conditions (stirring, pH, temperature, solvent:defatted meal ratio) resulted in 40% 70% protein isolation (Zhang et al., 2009; He et al., 2013b). Gerasimidis et al. (2007) prepared an edible cottonseed protein concentrate (72.2%) using a two-solvent extraction method utilizing acetone in aqueous and anhydrous form. Gossypol reduction was approximately 65%, producing a concentrate with oil and water absorption higher than wheat flours and good foaming properties. Ma et al. (2018) prepared cottonseed protein isolates (free gossypol contain ,0.012%) using different methods of solvent extraction (hot, cold, and supercritical). Isolates obtained by cold solvent extraction and supercritical fluid extraction showed good functional properties (high emulsifying capacities, high water/oil adsorption, and surface hydrophobicity) allowing their use as food ingredients. Overall, proteins isolated from gossypol-free CM could be used as food additives. However, more studies are required. 4.4.2.4 Sunflower Proteins Sunflower (Helianthus annuus L.) meal, a by-product of the sunflower oil industry, comprises 30% 50% protein (Weisz et al., 2009). Albumin (17% 30%) and globulins (mostly helianthinin protein, 300 350 kDa) are the major dominant storage proteins, although other minor proteins, oleosins included, are also described (Gonza´lez-Pe´rez, 2015). Lysine is the first limiting amino acid of sunflower proteins. Sunflower meal is mostly used as low-value animal feed. This is mainly due to the presence of phenolic compounds (1% 4%), like 5-O-caffeoylquinic acid (the most abundant) and caffeic acid (Weisz et al., 2009). Conventional vegetable protein extraction under alkaline condition causes polyphenol oxidation and simultaneous interaction of this compounds with sunflower proteins (Gonza´lez-Pe´rez, 2015). These interactions reduce protein digestibility and solubility, impart astringency and bitter taste, and affect the sensorial properties (mainly color) of the protein extract (Weisz et al., 2009). A novel pilot plant process using salt-assisted protein extraction under mild acidic conditions, combined with adsorption and ion exchange resin columns, was developed by Weisz et al. (2013) and Pickardt et al. (2015). This process prevents the protein polyphenol interaction, allows the removal and recovery of polyphenols, and leads to the production of light-colored sunflower protein isolates. Dephenolized protein isolates showed higher solubility, foaming properties, dispersibility, and emulsifying activity than protein isolates with higher phenolic content (Malik and Saini, 2017). Bioactivities associated with polyphenols and the good quality of sunflower protein could lead to the economic viability of sunflower meal utilization for human food consumption. 4.4.2.5 Palm Kernel Meal Palm kernel meal (PKM) is the by-product generated by oil extraction from the African oil palm (Elaeis guineensis Jacq.) (Alimon, 2004). Palm oil is extensively produced also in Central and South America as well as in East Asia (Sharmila et al., 2014). Palm oil and palm kernel oil are the two main marketable products obtained from African oil palm, representing 22% and 4% 6% of the fresh-fruit bunch weight, respectively (Boateng et al., 2008). Several by-products (fronds, trunks, press fiber, empty fruit bunches, kernel cake,

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kernel shells, and mill effluent) are generated from oil extraction and used for livestock feeding (Marini et al., 2005). PKM world production exceeded 9.5 million metric tons in 2017, with Indonesia and Malaysia producing together just over four-fifths of that. After a first stage of oil extraction from palm, the kernel is obtained. Crushed palm kernels are extracted in the second stage from which the PKM results (Sharmila et al., 2014). Several strategies are used in palm kernel oil extraction that generate the high-protein PKM, such as mechanical extraction, solvent extraction, prepressing followed by protein extraction, as well as hydrothermal techniques. More recently, supercritical carbon dioxide extraction has been shown to be an effective strategy to produce low-priced de-oiled PKM as a suitable source of protein and fiber for human and animal consumption (Saw et al., 2012; Boateng et al., 2013; Sharmila et al., 2014; Hossain et al., 2016). Chemical and therefore nutrient composition of PKM depend on a number of factors, such as the palm sources, efficiency of oil extraction from the kernel, the residual endocarp, and the oil extraction method (Onuh et al., 2010). Protein content of PKM ranges 14.4% 20%. It also contains a high amount of carbohydrates (50.3%) and crude fiber (16.7%). Nutritive values of PKM can be enhanced by biological processes such as solid-state fermentation with cellulolytic and hemicellulolytic bacterial cultures in order to increase the protein value and the availability of nutrients (Marini et al., 2005; Alshelmani et al., 2014). A protein concentrate can be obtained by extraction of ground PKM with alkali (1 N NaOH) followed by precipitation with HCl (pH 3.5), with a protein yield of around 55% 60% (Manaf, 2008). Although the isoelectric method and modifications to it are widely used, there is no universal or standard method for isolating proteins from PKM. Protein extraction can also be performed with alkaline (30 60 mM NaOH, 35 45 C) or saline solution (200 400 mM NaCl, pH 7 9) and drying at 50 C (Arifin et al., 2009). An alternative method used for PKM protein isolation is the extraction with sodium hexametaphosphate and further isoelectric precipitation of soluble protein at pH 3.7 (Chee and Ayob, 2013). Because of the low cost and high availability of PKM, it is used to partially substitute feed ingredients such as soybean and maize in livestock feeds, poultry broiler, swine, and freshwater fish (Zahari and Alimon, 2005). However, PKM is also a potential source of valuable components for human nutrition and raw materials for several industries. Searches for bioactive peptides that allow the generation of functional products with high added value from PKM have been performed. Peptides of variable molecular weight and antioxidant activity have been obtained after hydrolysis of PKM with different proteases (trypsin, flavourzyme, chymotrypsin, bromelain, alcalase, pepsin, and papain). It is noteworthy that, the use of papain as hydrolytic enzyme produced the hydrolysate with the highest antioxidant activity (Saw et al., 2012). Remarkably, PKM protein obtained by hexametaphosphate-assisted extraction shows better solubility at pH 7, as well as higher oil binding capacity and emulsion activity, but lower emulsion stability, foaming capacity, foaming stability, and water binding capacity, when compared to soybean protein isolate. Nevertheless, PKM protein obtained by hexametaphosphate-assisted extraction also displayed an essential amino acid profile limited in tryptophan. Consequently, it can be used as a complementary source by supplementing with a tryptophan-rich source (Chee and Ayob, 2013).

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The palm oil industry generates millions of tons of low cost PKM as by-product per year. PKM is widely used as a complement for animal feeding because of its high-protein content. However, despite being used as a source of bioactive antioxidant peptides, PKM isolated proteins have not being used for human consumption. There is a requirement for a more rigorous evaluation of the physicochemical properties of the protein extracted from PKM to successfully incorporate these proteins into food systems and products with high added value. 4.4.2.6 Peanut Meal The groundnut or peanut (Arachis hypogaea L.) is a legume native to South America (Devi et al., 2013). The peanut is the fifth most used vegetable source worldwide for the production of vegetable oil (Sibt-e-Abbas et al., 2015). Peanut by-products are rich in functional compounds like proteins, fiber, polyphenols, antioxidants, vitamins, and minerals, which can be included in many processed human foods, besides being used as a replacement for conventional components in livestock and fish diets (Arya et al., 2016; SantosDias et al., 2018). The residue generated after the extraction of peanut oil is called oil cake/meal, or peanut meal, which is obtained in the form of flakes or grits (Kain et al., 2009). This by-product is rich in crude protein (20% 45%) and contains about 6% of residual oil (Fapohunda, 2008; Kain and Chen, 2008). Peanut meal world production exceeded 7.3 million metric tons in 2017, with China and India together accounting for over 71%. It is used commonly for animal feeding; however, its incorporation at high levels results in poor growth because of the presence of antinutritional compounds (Ghosh and Mandal, 2015). It also represents an economical and underutilized by-product with essentially the same health and nutritional benefits as peanut, and possesses remarkable functional properties that are important for food processing and food product formulation (Kain and Chen, 2008). Peanut meal protein isolate is regularly obtained by alkali extraction at pH 8, followed by isoelectric precipitation at pH 4.5 (Jain et al., 2015). This protein isolate contains 86% protein. Due to their excellent functional properties, peanut meal protein isolates can be used in supplementation of several food products, also enhancing their nutritional value (Sibt-e-Abbas et al., 2015). Peanut meal is often processed to obtain defatted peanut flour, which is a cheap high-protein source with equal dietary attributes of peanut but reduced in fat. Defatted peanut meal flour contains 40% 60% protein, 20% 30% carbohydrate, 3.8% 7.5% crude fiber, and 4% 6% minerals (Devi et al., 2013). Protein from peanut defatted flour has been concentrated up to 72% by ultrafiltration after being treated with cellulase, and finally freeze dried (Jain et al., 2015). Peanut meal flours with high oil and water absorption are desirable for use in meats, sausages, breads, and cakes, whereas flours with high emulsifying and whipping capabilities are more suitable for salad dressing, soups, bologna, confectioneries, frozen desserts, and cakes (Kain and Chen, 2008). It is noteworthy that some of the functional properties of peanut meal flour can be modified by the processing and production methods. For example, peanut meal protein concentrate prepared using membrane technology showed superior functional and sensorial characteristics compared to acid-precipitated peanut protein isolate (Jain et al., 2015).

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4.4.2.7 Cashew Meal The cashew tree (Anacardium occidentale L.) is native to South and Central America. It is widely cultivated for its nuts and derived products throughout Australia, Asia, and Africa (Ogunwolu et al., 2010; Liu et al., 2018). Cashew nut production amounted to 4.28 million tons in 2015, with Nigeria, India, and Vietnam producing 53%. Cashew kernel is rich in lipids (40% 57%), carbohydrates (23% 25%), and high-quality proteins (20% 25%). Also, it is rich in monounsaturated (61%) and polyunsaturated (17%) fatty acids (Lima et al., 2012; Liu et al., 2018). During processing large amounts (around 30%) of cashew kernels are rejected because they are not suitable for sale. These full-fat and defatted rejected meals are rich in proteins and are used in animal feeding (Akande et al., 2015). Defatted flour is obtained by grinding cashew nuts and removing lipids with petroleum ether. Defatted flakes are air-dried to completely remove the solvent and finally, ground to obtain the defatted cashew flour (Liu et al., 2018). A protein isolate can be obtained by dispersing defatted flour in deionized water and adjusting pH to 9.0 before stirring for 2 hours. The suspension is centrifuged and the supernatant collected. Sediments are suspended again in water to repeat the extraction as described previously and supernatants are pooled and pH adjusted to pH 4.6. Precipitated proteins are recovered by centrifugation, suspended in deionized water, neutralized, dialyzed against cold water, and freezedried (Liu et al., 2018). Osborne fractions of cashew meal have also being obtained using a previously reported method (Deng et al., 2011). Results have shown that Osborne fractionation is practical to preliminarily purify cashew nut meal protein where the main fractions are globulins (51.4%), glutelins (23.2%), and albumins (22.9%), whereas prolamins represent a very small proportion (2.5%) (Liu et al., 2018). Functional properties of cashew protein isolate and concentrate as well as albumin, globulin, and glutelin fractions have been evaluated and the results were comparable to those of peanut, lupin, and soybean proteins currently used as functional ingredients in numerous food products (Ogunwolu et al., 2009; Liu et al., 2018). According to FAO/WHO recommendations, the content of essential amino acids lysine, isoleucine, and valine in albumin, globulin, and glutelin, as well as in cashew nut protein isolate can satisfy young children’s requirements (Liu et al., 2018). Increased global production of cashew makes necessary the exploitation of cashew meal as a cheap source of protein concentrates, whereas isolated fractions with interesting functional properties may be relevant for the food industry.

4.4.3 Other Sources of Plant Proteins Alongside the usual sources of plant oil (e.g., soybean, canola, cotton, sunflower, palm, and peanut), there are other oil seeds like sesame, pecan, coconut, and macadamia nut. Also, there are other less extensively exploited plant oil sources like neem seed (Indica azadirachta), hemp seed (Cannabis sativa), and several cucurbitaceous seeds (Cucurbita maxima, C. pepo, C. moshata). From the processing of all of them, by-products are obtained which represent alternative plant protein sources useful as food for livestock, fishes, poultry, and human, as well as being sources of bioactive peptides (Usman et al., 2005; Aguilar et al., 2011; Chambal et al., 2012; Ranganayaki et al., 2012; Van Ryssen et al., 2014; de Menezes Lovatto et al., 2015; Rezig et al., 2016;

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Ozuna and Leo´n-Galva´n, 2017; Hadnaðev et al., 2018; Marchetti et al., 2018). Studying molecular and functional properties of such protein concentrates/isolates will determine their suitability as functional food ingredients (Liu et al., 2018). Oils extracted from castor bean (Ricinus communis) seeds and Jatropha curcas are widely used for biodiesel production. Castor bean seed meal is rich in proteins but cannot be used for animal feed because of the presence of toxic components like ricin, ricinin, agglutinin, and allergen CB-1-A (Madeira et al., 2011). However, protein can be extracted and concentrated to be used in the production of biodegradable materials (Lacerda et al., 2014). Due to the presence of toxic and antinutritional compounds, J. curcas seed meal (60% 63% protein) and oil are not suitable for animal or human consumption. However, a nontoxic J. curcas genotype not containing phorbol esters, but containing insignificant amounts of curcin that are not enough to cause toxic effects has been reported, and their seeds are traditionally used as food in Me´xico (He et al., 2011; Perea-Domı´nguez et al., 2017; Leo´n-Villanueva et al., 2018). By-products of fruit industrialization are also of current interest, since as an outcome of fruit processing, the seeds, peel, rind, and unusable pulp are commonly discarded (Reis et al., 2012). As an example, the residues of jackfruit (Artocarpus heterophyllus) constitute 70% of the fruit weight, whereas seeds may represent 8% 15% and contain 18% 37% protein, depending on the fruit variety. Functional and nutritive properties of jackfruit seed protein isolate have been determined, showing a good balance of essential amino acids and good functional properties. Therefore, it can be a novel protein source suitable to be added to breads, cakes, beverages, ice cream, sausage, and meat products (Ulloa et al., 2017).

4.5 CONCLUDING REMARKS The growing interest in plant proteins as an alternative to animal proteins is due to their comparative low cost as well as the increase in consumers’ demands originating from health and environmental concerns, and vegetarianism trends. Numerous residues coming from the food industry, especially those from vegetable oil extraction are low-cost plant protein sources. Due to the low solubility in water, conventional methods of recovering plant protein include the alkaline extraction and isoelectric precipitation. The classical extraction presents some drawbacks, for example, low yields and using reagents or conditions that can damage biomolecules, in addition to the disposal or final handling of chemicals representing environmental risks. Thus, developing sustainable techniques for extracting plant proteins from conventional and unconventional sources is a current subject.

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