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Changes in physicochemical and functional properties of whey protein concentrate upon succinylation
Author(s) -
Shilpashree Bosayya Govindaraju,
Arora Sumit,
Sharma Vivek,
Chawla Prince,
Vakkalagadda Ravikumar
Publication year - 2017
Publication title -
international journal of dairy technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.061
H-Index - 53
eISSN - 1471-0307
pISSN - 1364-727X
DOI - 10.1111/1471-0307.12321
Subject(s) - succinylation , succinic anhydride , chemistry , solubility , lysine , emulsion , whey protein , viscosity , chromatography , food science , organic chemistry , biochemistry , materials science , amino acid , composite material
The highest degree of succinylation was achieved at the level of 6 moles of succinic anhydride/mole of lysine in whey protein concentrate ( WPC ). Structural modification of protein or the presence of a high negative charge on the surface of protein upon succinylation exposed buried hydrophobic sites. The solubility of succinylated protein derivatives increased at alkaline pH but decreased at acidic pH values as compared to native WPC . The physicochemical properties of succinylated protein derivatives, such as water– and oil– binding capacity, viscosity and emulsion properties increased significantly ( P < 0.05) compared to native WPC , whereas, foaming stability reduced significantly ( P < 0.05) and there was no change in the foaming capacity.