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Functional properties of protein hydrolysates from pea ( Pisum sativum , L ) seeds
Author(s) -
Barac Miroljub,
Cabrilo Slavica,
Stanojevic Sladjana,
Pesic Mirjana,
Pavlicevic Milica,
Zlatkovic Branislav,
Jankovic Miodrag
Publication year - 2012
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2012.02993.x
Subject(s) - pea protein , papain , solubility , protease , proteases , pisum , sativum , hydrolysis , enzyme , food science , chemistry , biology , chromatography , biochemistry , botany , organic chemistry
Summary 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.