Improvement of Hairtail Surimi Gel Properties by NADPH-Sulfite Reductase, Recombinant Cystatin, and Microbial Transglutaminase

Effects of nicotinamide dinucleotide phosphate (NADPH)-sulfite reductase, recombinant cystatin, and microbial transglutaminase (MTGase) or their combination on hairtail surimi quality were investigated. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that adding NADPH-sul...

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Veröffentlicht in:	Journal of food science 2002-10, Vol.67 (8), p.3152-3158
Hauptverfasser:	Hsieh, J.F, Tsai, G.J, Jiang, S.T
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences chickens crosslinking Enzymes Fish Fish and seafood industries Food industries Food products Food science Fundamental and applied biological sciences. Psychology gel property gels hairtail surimi MTGase myosin NADP (coenzyme) NADPH-sulfite reductase nicotinamide polyacrylamide gel electrophoresis protein-glutamine gamma-glutamyltransferase Quality recombinant cystatin surimi
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Beschreibung
Zusammenfassung:	Effects of nicotinamide dinucleotide phosphate (NADPH)-sulfite reductase, recombinant cystatin, and microbial transglutaminase (MTGase) or their combination on hairtail surimi quality were investigated. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that adding NADPH-sulfite reductase could effectively recover native myosin. Apparent cross-linking of hairtail myosin during the setting process was observed with added MTGase, while myosin degradation on the heating process was substantially retarded with recombinant chicken cystatin. The combined use of NADPH-sulfite reductase, recombinant chicken cystatin, and MTGase exhibited a greater effect on improving hairtail surimi quality.
ISSN:	0022-1147 1750-3841
DOI:	10.1111/j.1365-2621.2002.tb08875.x