Premium
Improvement of the Functionalities of Soy Protein Isolate through Chemical Phosphorylation
Author(s) -
SUNG HSIENYI,
CHEN HSIENIJER,
LIU TINYIN,
SU JONGCHING
Publication year - 1983
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1983.tb14882.x
Subject(s) - soy protein , chemistry , phosphorylation , bioavailability , lysine , aqueous solution , serine , solubility , chromatography , food science , biochemistry , organic chemistry , amino acid , biology , bioinformatics
A method of chemical phosphorylation was developed to modify soy protein so as to improve its functional properties. The reaction was carried out by incubating soy protein isolate and cyclic sodium trimetaphosphate in an aqueous solution at pH 11.5 and 35°C for about 3 hours. The reactions ensued were the phosphoesterification of serine residues and the phosphoramidation of lysine residues in soy protein. The phosphorylated soy protein isolate prepared there‐from exhibited much improved functional properties in terms of aqueous solubility, water‐holding capacity, emulsifiability and whippability. The nutritive bioavailability of soy protein isolate was not impaired by phosphorylation.