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Inducibility of Rat Liver Drug-Metabolizing Enzymes as an Index of Food-Screeing for Safety Assessment
Authors:Yasuo Kitagawa  Etsuro Sugimoto
Institution:1. Institute for Biochemical Regulation, Faculty of Agriculture;2. Nagoya University, Chikusa-ku, Nagoya 464, Japan
Abstract:D-Lactate dehydrogenase (D-LDH) from Pediococcus pentosaceus ATCC 25745 was found to produce D-3-phenyllactic acid from phenylpyruvate. The optimum pH and temperature for enzyme activity were pH 5.5 and 45 °C. The Michaelis-Menten constant (K m), turnover number (k cat), and catalytic efficiency (k cat?K m) values for the substrate phenylpyruvate were estimated to be 1.73 mmol/L, 173 s?1, and 100 (mmol/L)?1 s?1 respectively.
Keywords:D-lactate dehydrogenase" target="_blank">D-lactate dehydrogenase  D-3-phenyllactic acid" target="_blank">D-3-phenyllactic acid  phenylpyruvate  Pediococcus pentosaceus  characterization
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