Transglutaminase from Streptoverticillium ladakanum and application to minced fish product |
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Authors: | GUO-JANE TSAI SHANG-MAY LIN SHANN-TZONG JIANG |
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Affiliation: | The authors are affiliated with the Dept. Of Marine Food Science, National Taiwan Ocean Univ., Keelung, Taiwan 202, ROC. Direct inquiries to Dr. Shann-Tzong Jiang. |
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Abstract: | The transglutaminase (TGase) from Streptoverticillium ladakanum was purified to electrophoretic homogeneity after ammonium sulfate fractionation and Blue Sepharose Fast Flow chromatography. The molecular weight of the purified TGase was 30.5 kDa estimated by Superdex 75HR gel filtration, and 37.5 kDa by SDS-PAGE. This enzyme, with optima at pH at 6.0 and 50°C was very stable at pH 5.0–7.0. It was strongly inhibited by PCMB, PMSF, Pb2+, Zn2+ and Cu2+, but not affected by EDTA and Ca2+. This suggested that the purified TGase was calcium-independent and its active center contained cysteine. It catalyzed the crosslinking of fish myosin heavy chain and substantially increased the gel strength of mackerel surimi. |
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Keywords: | microbial transglutaminase mackerel surimi Streptoverticillium ladakanum |
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