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Purification and characterization of transglutaminase from Japanese oyster (Crassostrea gigas)
- Kumazawa, Y., Sano, K., Seguro, K., Yasueda, H., Nio, N., Motoki, M.
- Journal of agricultural and food chemistry 1997 v.45 no.3 pp. 604-610
- Crassostrea gigas, ammonium sulfate, calcium chloride, chromatography, fractionation, gills, lysine, manufacturing, molecular weight, oysters, pH, protein-glutamine gamma-glutamyltransferase, sodium chloride, temperature
- A total of 73% transglutaminase (TGase) activity was detected in the gills and mantles of Japanese oysters (Crassostrea gigas), and TGase was purified by ammonium sulfate fractionation, followed by column chromatography. Two types of TGase with molecular weights of the 84 000 (TG-1) and 90 000 (TG-2) were obtained. The optimum pH was 8.0 for both TGases, and the optimum temperature for TG-1 and TG-2 was 40 and 25 degrees C, respectively. The activity of TG-1 increased with NaCl concentrations, whereas that of TG-2 was inhibited by NaCl. In the absence of NaCl, the activity of TG-1 increased with CaCl2 concentrations up to 100 mM, but the concentration required to express full activity of TG-2 was 25 mM. This CaCl2 concentration was lowered to 25 mM for TG-1 in the presence of 0.5 M NaCl, but not changed for TG-2. The epsilon(gamma-glutamyl)lysine was not detected in fresh oyster but was detected in processed oyster, suggesting the possibility that the intrinsic TGases react in the manufacturing process of oyster products.