嗜冷海洋细菌中乳酸脱氢酶的特性

Mitchell P, Yen H C, Mathemeier P F

Appl Environ Microbiol. 1985 May;49(5):1332-4. doi: 10.1128/aem.49.5.1332-1334.1985.

Lactate dehydrogenase (EC 1.1.1.27) from Vibrio marinus MP-1 was purified 15-fold and ammonium activated. The optimum pH for pyruvate reduction was 7.4. Maximum lactate dehydrogenase activity occurred at 10 to 15 degrees C, and none occurred at 40 degrees C. The crude-extract enzyme was stable between 15 and 20 degrees C and lost 50% of its activity after 60 min at 45 degrees C. The partially purified enzyme was stable between 8 and 15 degrees C and lost 50% of its activity after 60 min at 30 degrees C. The thermal stability of lactate dehydrogenase was increased by mercaptoethanol, with 50% remaining activity at 42 degrees C.

从海弧菌MP-1中纯化出的乳酸脱氢酶（EC 1.1.1.27）经15倍纯化并被铵激活。丙酮酸还原的最适pH为7.4。乳酸脱氢酶的最大活性出现在10至15摄氏度，40摄氏度时无活性。粗提酶在15至20摄氏度之间稳定，在45摄氏度下60分钟后活性丧失50%。部分纯化的酶在8至15摄氏度之间稳定，在30摄氏度下60分钟后活性丧失50%。巯基乙醇提高了乳酸脱氢酶的热稳定性，在42摄氏度下仍保留50%的活性。