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KINETICS and MECHANISM of NONENZYMATIC DEAMIDATION of SOY PROTEIN
Author(s) -
ZHANG JIB,
LEE TUNG CHING,
HO CHITANG
Publication year - 1993
Publication title -
journal of food processing and preservation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.511
H-Index - 48
eISSN - 1745-4549
pISSN - 0145-8892
DOI - 10.1111/j.1745-4549.1993.tb00730.x
Subject(s) - deamidation , chemistry , soy protein , kinetics , asparagine , glutamine , chromatography , biochemistry , amino acid , enzyme , physics , quantum mechanics
Nonenzymatic deamidation of glutamine and asparagine residues of soy protein in aqueous solutions of varying pH (3.0, 5.0, 7.0, 9.0 and 11.0) at different temperatures (100C, 115C and 130C) was monitored over a period of time. the deamidation of soy protein followed first‐order kinetics. the activation energies (Ea) of soy protein deamidation at different pHs ranged from 14 to 27 Kcal/mol. the activation energies were highly pH‐dependent and decreased very sharply as the pH went up from pH 5 to pH 11.