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Improvement of Hairtail Surimi Gel Properties by NADPH-Sulfite Reductase, Recombinant Cystatin, and Microbial Transglutaminase
Authors:J.-F. Hsieh    G.-J. Tsai    S.-T. Jiang
Affiliation:Authors Hsieh, Tsai, and Jiang are with the Dept. of Food Science, National Taiwan Ocean Univ., Keelung 202, Taiwan. Direct inquiries to author Jiang (E-mail: ).
Abstract:ABSTRACT: 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.
Keywords:NADPH-sulfite reductase    recombinant cystatin    MTGase    gel property    hairtail surimi
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