Soy protein modification: A review

Barać, Miroljub B.; Stanojevic, P Sladjana; Jovanović, Tatjana; Pesic, B Mirjana

doi:10.2298/apt0435003b

Cited by 64 publications

(37 citation statements)

References 57 publications

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“…Techno-functional properties of pea protein isolates can be improved by chemical, physical and enzymatic treatments. From the standpoint of safety, the most appropriate method for modification of legume protein properties is limited proteolysis (61). Peptides produced by partial proteolysis have smaller molecular size and less compact structure than the original proteins.…”

Section: Limited Proteolysis As a Methods For Improvement Of Techno-fumentioning

confidence: 99%

Techno-functional properties of pea (Pisum sativum) protein isolates: A review

Barać¹,

Pesic²,

Stanojević³

et al. 2015

Acta per tech

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Due to high nutritive quality, good techno-functional properties and low cost, legume protein products are becoming the most appropriate alternative to protein products of animal origin. In food industries, these products are usually used as techno-functional additives which provide specific characteristics of final food products. Legume proteins are commonly used as flour, concentrates, and isolates. The greatest application on industrial scale has soy proteins, and to a lesser extent, in the past 20 years, pea protein isolates. The modest use of pea protein is partly a result of insufficient information relating to their techno-functional properties. This paper is an overview of techno-functional properties of pea proteins and their isolates. Also, the paper deals with the possible use of limited enzymatic hydrolysis as a method for the improvement of their techno-functional properties.2 tein isolates, whereas some other (5,13,14) pointed out better properties of pea isolates. Variations in the results among different studies could be due to the differences in the protein purity of the studied samples, method of protein isolation, the specific conditions used for the tests, as well as the different processing conditions (7,15). Furthermore, significantly different functionalities among pea isolates were observed. Maninder et al. (16) and Barac et al. (6,17) attributed this to the different ratio of the major proteins, which is in turn influenced by genotype characteristics, environmental conditions, and processing conditions (10,(18)(19)(20). To avoid the difference caused by different processing conditions, Barac et al. (15) prepared and compared pea, soybean and adzuki isolates under the same conditions. The results of this investigation showed that techno-functional properties of the isolates prepared from different species depended on several factors such as: choice of species and varieties, preparation conditions, and the pH value at which specific properties were tested. STORAGE PEA PROTEINSPea seeds contain about 22-23% proteins. The majority of pea proteins are globulins and albumins, which represent about 80% of total seed protein content. Albumins represent 18-25% and globulins 55-65% of total proteins (21). All globulins and some of albumins are storage proteins, which are used as nitrogen sources for the new embryos after seed germination (22).Major pea storage proteins, legumin, vicilin and convicilin are globulins and represent 65-85% of total proteins (23). According to sedimentation properties these proteins are classified into two fractions, 7S (vicilin, convicilin) and 11S fraction (legumin). Molecular forms of the three major proteins are presented in Figure 1. Figure 1. Molecular forms of legumin, vicilin and convicilin (22) APTEFF, 46, 1-269 (2015) 6 Alternatively, the isoelectric precipitation step can be substituted by ultrafiltration. The use of ultrafiltration increases the yield of isolates and change their composition. Isolates prepared by ultrafiltration contain 90-94% of protei...

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Section: Limited Proteolysis As a Methods For Improvement Of Techno-fumentioning

confidence: 99%

Techno-functional properties of pea (Pisum sativum) protein isolates: A review

Barać¹,

Pesic²,

Stanojević³

et al. 2015

Acta per tech

Self Cite

100

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“…For that reason, only SDS-patterns of thermally treated isolates at pH 8.0 and pH 3.0 were presented. Heating plant proteins above 80°C causes dissociation of their quaternary structures, denatures their subunits, and promotes the formation of more or less soluble protein aggregates via electrostatic, hydrophobic and disulfide interchange mechanisms (Barac et al 2004). Thermal treatment enhanced solubility of major adzuki proteins, whereas reduced solubility of soy protein isolates at pH 8.0 as evident on SDS-PAGE patterns (Fig.…”

Section: Protein Solubilitymentioning

confidence: 99%

“…Boye et al (2010b) reviewed the influence of processing techniques including alkaline extraction/isoelectric precipitation, acid extraction, water extraction, micellization, ultrafiltration and enzymatic modification on yield, characteristics and functionality of pea, bean and chickpea protein isolates. Also, Barac et al (2004) reviewed functionality of soy protein isolates and methods for its improvement. Both groups of authors suggested that besides other factors (e.g.…”

Section: Introductionmentioning

confidence: 99%

Comparative study of the functional properties of three legume seed isolates: adzuki, pea and soy bean

et al. 2014

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The aim of this work was to compare functional properties including solubility, emulsifying and foaming properties of native and thermally treated adzuki, soy and pea protein isolates prepared under the same conditions. These functional properties were tested at four pH values: pH 3.0, pH 5.0, pH 7.0 and pH 8.0. The lowest solubility at all pH values were obtained for isolate of adzuki whereas isolates of soybean had the highest values at almost all pHs. Thermal treatment reduced solubility of soy and pea isolates at all pH values, whereas solubility of adzuki isolate was unchanged, except at pH 8. Native isolate of adzuki had the best emulsifying properties at pH 7.0 whereas at the other pH values some of native pea and soybean protein isolates were superior. After thermal treatment, depending on tested pH and selected variety all of three species could be a good emulsifier. Native soy protein isolates formed the most stable foams at all pHs. Thermal treatment significantly improved foaming properties of adzuki isolate, whereas reduced foaming capacity of soy and pea isolates, but could improve foam stability of these isolates at specific pH. Appropriate selection of legume seed as well as variety could have great importance in achievement of desirable functional properties of final products. All three tested species could find specific application in wide range of food products.

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“…Soy proteins contain four protein fractions that are classified according to their sedimentation properties into: 2 s, 7 s, 11 s and 15 s which represent, respectively, 8 g/100 g, 35 g/100 g, 52 g/100 g and 5 g/100 g of the total protein content (Bara et al, 2004;Kinsella, 1979). Soy protein isolate contains 90% protein, its major components being 7 s globulin or b-conglycinin and 11 s globulin or glycinin (Petruccelli and Añon, 1995;Beleciu and Moraru, 2013).…”

Section: Introductionmentioning

confidence: 99%