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DIFFERENT ARRANGEMENT OF ɛ‐(γ‐GLUTAMYL)LYSINE CROSS‐LINKING IN ALASKA POLLOCK ( THERAGRA CHALCOGRAMMA ) SURIMI PROTEINS BY STREPTOVERTICILLIUM AND ENDOGENOUS TRANSGLUTAMINASES DURING SUWARI PROCESS
Author(s) -
SATO KENJI,
TANAKA CHIE,
KOTARU MAKOTO,
YOSHKAWA HIDEKI,
KAWABATA MAKOTO,
KEUCHI TSUNEO,
SATO KENTA,
NAKAMURA YASUSHI,
OHTSUKI KOZO
Publication year - 2001
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2001.tb00748.x
Subject(s) - lysine , chemistry , pollock , food science , endogeny , biochemistry , biology , fishery , amino acid
The objective of the present study is to compare the protein cross‐linking reaction in Alaska pollock surimi that is catalyzed by a commercially available microbial transglutaminase and by endogenous Alaska pollock transglutaminase. The endogenous transglutaminase was inhibited by EGTA and activated by CaCl 2 The microbial transglutaminase was added to the salted surimi with and without EGTA and CaCl 2 . These surimi pastes were incubated at 25C up to 24 h followed by cooking at 90C. The resultant gels were fractionated into soluble and insoluble (aggregate) fractions by SDS‐urea extraction. Compositional analysis revealed that the aggregate consisted predominantly of cross‐linked myosin heavy chain. The distribution of ɛ‐(γ‐glutamyl)lysine isopeptide in the soluble and aggregate fractions andpeptide mapping analyses of the aggregate fraction demonstrate that the formation of isopeptide cross‐links in Alaska pollock surimi proteins during suwari process differs when catalyzed by the microbial transglutaminase and endogenous transglutaminase.