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

Abstract

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...

Model system evaluation of the effects of pea and pH on the emulsion properties of beef

“…As shown in Figure 2, ES increased rapidly as pH moved away from the isoelectric point of the meat proteins. Moreover, the main pea proteins have very low emulsion stability in the pI (isoelectric point) range (Barać et al, 2015). Varying pH, ionic species, and ionic strength cause pea proteins to form different network structures (Munialo et al, 2014).…”

“…There is a significant relationship between EA and pH values (Neto et al, 2001) affecting the solubility of protein and polysaccharide and leading to differences in net electrical charge. Barać et al (2015) suggested that the emulsification activity is a minimum in the isoelectric point range of major pea proteins. Moreover, they reported that as the pH is moved away from pI, the emulsifying properties improve due to intensive dissociation, which is more evident in the case of legumin (Neto et al, 2001).…”

“…Pea products can be added to the formulations of food products to improve product quality and technological properties. The technological properties of pea proteins have a positive effect on emulsification (Franco et al, 2000;Gharsallaoui et al, 2009;Barać et al, 2015). Pea proteins contain soluble proteins with good gel formation, water-binding, and emulsification properties required for meat products (Tarté, 2009).…”

“…Pea proteins contain soluble proteins with good gel formation, water-binding, and emulsification properties required for meat products (Tarté, 2009). Protein solubility and emulsion properties of meat products are closely related (Schut, 1976;Barać et al, 2015). However, protein solubility is closely related to extrinsic factors, such as pH, ionic strength, and temperature (Söderberg, 2013;Bolontrade et al, 2013).…”

Bioactive Peptides from Legumes as Anticancer Therapeutic Agents

“…Robles-Ramírez, et al [18] evaluated the effect of germinated soy protein on the growth of HeLa cervical cancer cells in female athymic mice. They observed that teins [40]. A diet high in dry pea has been demonstrated to be effective in lowering the incidence of colon cancer, type-2 diabetes, LDL-cholesterol and heart disease [36].…”