Tehno-funkcionalne osobine izolata proteina graška

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.Zahvaljujući visokoj nutritivnoj vrednosti, dobrim tehno-funkcionalnim karakteristikama i niskoj ceni, proteini leguminoza postaju najprihvatljivija alternativa za proteinske proizvode animalnog porekla. U industriji hrane ovi proizvodi najčešće se koriste kao tehno-funkcionalni aditivi kojima se obezbeđuje neka od karakteristika finalnog proizvoda. Proteini leguminoza najčešće se koriste kao proteinska brašna, koncentrati i izolati. U industrijskim razmerama najveću primenu imaju proteini soje i u znatno manjoj meri, u poslednjih 20 godina, proteinski izolati graška. Ređa upotreba proteina graška delom je posledica još uvek nedovoljno informacija o njihovim tehno-funkcionalnim karakteristikama. Ovaj rad predstavlja pregled tehno-funkcionalnih karakteristika proteina graška i njegovih izolata. Takođe, u ovom radu razmatra se i delimična proteoliza kao metod za poboljšanje tehno-funkcionalnih karakteristika proteina graška

Functional Properties of Pea (Pisum sativum, L.) Protein Isolates Modified with Chymosin

In this paper, the effects of limited hydrolysis on functional properties, as well as on protein composition of laboratory-prepared pea protein isolates, were investigated. Pea protein isolates were hydrolyzed for either 15, 30 and 60 min with recombined chymosin (Maxiren). The effect of enzymatic action on solubility, emulsifying and foaming properties at different pH values (3.0; 5.0; 7.0 and 8.0) was monitored. Chymosin can be a very useful agent for improvement of functional properties of isolates. Action of this enzyme caused a low degree of hydrolysis (3.9–4.7%), but improved significantly functional properties of pea protein isolates (PPI), especially at lower pH values (3.0–5.0). At these pH values all hydrolysates had better solubility, emulsifying activity and foaming stability, while longer-treated samples (60 min) formed more stable emulsions at higher pH values (7.0, 8.0) than initial isolates. Also, regardless of pH value, all hydrolysates showed improved foaming ability. A moderate positive correlation between solubility and emulsifying activity index (EAI) (0.74) and negative correlation between solubility and foam stability (−0.60) as well as between foam stability (FS) and EAI (−0.77) were observed. Detected enhancement in functional properties was a result of partial hydrolysis of insoluble protein complexes

Functional properties of protein hydrolysates from pea (Pisum sativum, L) seeds

The aim of this study was to investigate the effects of partial enzymatic hydrolysis on functional properties of two different pea protein isolates obtained from two pea genotypes, Maja and L1. Papain and commercial protease (Streptomyces griseus protease) were used for protein modification. Solubility, emulsifying and foaming properties were estimated at four different pH values (3.0, 5.0, 7.0 and 8.0). Papain increased solubility of L1 pea protein isolate at pH 3.0, 5.0 and 8.0, emulsifying properties and foaming capacity at all pH values. Otherwise, papain increased solubility of Maja pea protein isolate only at pH 8.0. This pea protein isolate modified with both enzymes formed emulsions with improved stability at lower pH (3.0, 5.0). The commercial protease-prepared pea protein isolates showed generally low solubility and different emulsifying and foaming properties. Proper selection of enzyme, conditions of hydrolysis and genotypes could result in production of pea protein isolates with desirable functional properties