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World J Microbiol Biotechnol. 1994 Jul;10(4):385-7. doi: 10.1007/BF00144456.
Kluyveromyces marxianus had a higher specific activity of diacetyl reductase (EC 1.1.1.5) than all other organisms previously reported. The enzyme was NADH-dependent and irreversibly catalysed the conversion of diacetyl to acetoin with an optimum pH of 7.0. It was stable at 40°C but lost 50% of its activity at 50°C in 30 min. The K m and V max values for diacetyl were 1.8 mM and 0.053 mM/min, respectively.
马克斯克鲁维酵母的二乙酰还原酶(EC 1.1.1.5)比以往报道的所有其他生物的比活都要高。该酶依赖 NADH,不可逆地催化二乙酰转化为乙酰醇,最适 pH 值为 7.0。它在 40°C 时稳定,但在 50°C 时 30 分钟内失去 50%的活性。二乙酰的 K m 和 V max 值分别为 1.8mM 和 0.053mM/min。