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分支杆菌Mycobacterium fortuitum HCCB003 Δ~1-脱氢酶的初步研究 被引量:5

Studies on Δ~1-dehydrogenase of Mycobacterium fortuitum HCCB003
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摘要 研究了分支杆菌MycobacteriumfortuitumHCCB 0 0 3无细胞PBS抽提液对底物 4AD和ADD的转化 ,发现该菌株中同时存在Δ1 脱氢酶和Δ1 还原酶 ,但前者的催化活性远高于后者。同时研究了不同温度及有关金属离子对Δ1 脱氢酶活力的影响 ,发现 2 8℃为该酶的最适温度 ,以及一定浓度的Fe2 + 、Mn2 + 、Zn2 + 、和Ca2 + 对该酶具有激活作用。 The biotransformation process of 4AD and ADD using the cell free system by Mycobacterium fortuitum HCCB 003 was studied. The results showed that there existed Δ 1 dehydrogenase and Δ 1 reductase in this strain simultaneously and the activity of the former enzyme was much more higher than that of the latter one. Comparing the effects of different temperature and metal ions on the activity of Δ 1 dehydrogenase, it was found that the optimal temperature was 28℃ and Fe 2+ , Mn 2+ , Zn 2+ , Ca 2+ had some activation for this enzyme at a suitable concentration.
出处 《工业微生物》 CAS CSCD 北大核心 2003年第3期33-35,共3页 Industrial Microbiology
关键词 分支杆菌 △^1-脱氢酶 △^1-还原酶 金属离子 发酵 Mycobacterium fortuitum Δ 1 dehydrogenase metal ions
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  • 1Trit Granot, Yair Aharonowitz, Amihay Freeman. Cosolvent effeet on Δ^1 -steriod-reductase activity of free and PAHH entrapped Mycobacterium fortuitum sp. NRRL-3805 cells. Appl Microbiol Biotechnol. 1988, 27 : 457 - 463.
  • 2Goren T, Hamik M, Rimon S et al. 1-ene-steriod-reductase of Mycobacterium fortuitum sp. NRRL-3805. J Steroid Biochem.1983, 19(6) : 1789- 1797.

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