Premium
Enhancement of Peptidoglutaminase Deamidation of Soy Protein by Heat Treatment and/or Proteolysis
Author(s) -
HAMADA JAMEL S.,
MARSHALL WAYNE E.
Publication year - 1988
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.1365-2621.1988.tb13546.x
Subject(s) - deamidation , chemistry , proteolysis , soy protein , hydrolysis , cysteine , peptide bond , biochemistry , chromatography , amide , disulfide bond , calpastatin , organic chemistry , food science , calpain , amino acid , enzyme
The limited deamidating ability of B. circulans peptidoglutaminase towards soy protein was increased 27‐fold by protein hydrolysis and altering soy protein conformation by moist heat. Adding disulfide bond reducing agents such as cysteine or sodium sulfite or salts such as NaCl or KC1 to the reaction mixture had little or no effect on deamidation. However, heat treatment at 100°C for 15 min, both before and after Alcalase proteolysis, rendered soy protein very susceptible to amide hydrolysis by peptidoglutaminase.