首页 | 本学科首页   官方微博 | 高级检索  
     

酿酒酵母中的D-(-)-扁桃酸脱氢酶
引用本文:严芬,郭养浩,林木仙,刘盈盈. 酿酒酵母中的D-(-)-扁桃酸脱氢酶[J]. 药物生物技术, 2007, 14(1): 43-47
作者姓名:严芬  郭养浩  林木仙  刘盈盈
作者单位:福州大学药物生物技术和工程研究所,福建,福州,350002
摘    要:酿酒酵母BY1.1b对苯乙酮酸不对称还原成D-(-)-扁桃酸的反应具有高度的催化还原活性和光学选择性。采用超声波细胞破碎、硫酸铵沉淀、DEAE-Sepharose FF离子交换层析及Sephacryl S-200分子筛层析等步骤,从酵母BY1.1b中分离纯化得到D-(-)-扁桃酸脱氢酶。该酶的相对分子质量约60000。该酶的生物合成模式为非细胞生长偶联型和非底物诱导型。该酶与酵母醇脱氢酶、马肝醇脱氢酶、乳酸脱氢酶及丙酮酸脱氢酶的底物特异性具有显著差别,是一种新型的脱氢酶。

关 键 词:酿酒酵母  D-(-)-扁桃酸脱氢酶  纯化  底物特异性
文章编号:1005-8915(2007)01-0043-05
修稿时间:2006-08-182006-11-08

D -(-)-Mandelate Dehydrogenase from Saccharomyces Cerevisiae
YAN Fen,GUO Yang-hao,LIN Mu-xian,LIU Ying-ying. D -(-)-Mandelate Dehydrogenase from Saccharomyces Cerevisiae[J]. Pharmaceutical Biotechnology, 2007, 14(1): 43-47
Authors:YAN Fen  GUO Yang-hao  LIN Mu-xian  LIU Ying-ying
Affiliation:Institute of Pharmaceutical Biotechnology and Engineering, Fuzhou University, Fuzhou 350002, China
Abstract:Saccharomyces cerevisiae sp. strain BY1.1b showed high bioreduction activity and optic selectivity for the asymmetric bioreduction of benzoylformate to form D-(-)-mandelate (D-(-)-MA). D-(-)-mandelate dehydrogenase (D-(-)-MDH) was isolated and purified from BY1.1b by a combination of ultrasonic process, ammonium sulfate precipitation, DEAE-Sepharose Fast Flow anion-exchange chromatography and Sephacryl S-200 gel filtration chromatography. The molecular weight of D-(-)-MDH was 60000. The biosynthesis of enzyme is irrelative with the growth of yeast cell and non-inducement of substrate. D-(-)-MDH from Saccharomyces cerevisiae sp. strain BY1.1b is a novel dehydrogenase, which is distinct with other dehydrogenases in substrate specificity.
Keywords:Saccharomyces cerevisiae   D-(-)-mandelate dehydrogenase   Purification   Specificity
本文献已被 CNKI 维普 万方数据 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号