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Cross‐Linking of α s‐1 Casein by Sodium Hypochlorite
Author(s) -
MATOBA TERUYOSHI,
SHIONO TAIICHI,
KITO MAKOTO
Publication year - 1985
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.1365-2621.1985.tb10578.x
Subject(s) - sodium hypochlorite , succinylation , chemistry , polymerization , casein , lysine , hypochlorite , hydrolysate , trichloroacetic acid , formaldehyde , amino acid , organic chemistry , biochemistry , polymer chemistry , hydrolysis , polymer
α s‐1 Casein was polymerized in the presence of sodium hypochlorite (NaOCl). The polymerization was suppressed by succinylation of the protein. Dityrosine and α‐aminoadipic acid were detected in the hydrolysate of the reacted proteins. A carbonyl group was detected in the reaction product of acetyl lysine methylester and NaOCl. The Schiff base formation between lysine and a‐aminoadipic δ‐semialdehyde residues, and dityrosine formation may clarify the mechanism of polymerization. The chemical modification of proteins by NaOCl is expected to be useful for improving the functional properties of food proteins, since polymerization by NaOCl could occur under mild conditions (NaOCl cone, <0.05%; time, <5 min; at 37°C and pH 7‐9).