Characterization of cold-active dehydrogenases for secondary alcohols and glycerol in psychrotolerant bacteria isolated from Antarctic soil

被引:6
作者
Stibor, M
Potocky, M
Pícková, A
Karasová, P
Russell, NJ
Králová, B
机构
[1] Inst Chem Technol, Fac Food & Biochem Technol, Dept Biochem & Microbiol, Prague 16628, Czech Republic
[2] Univ London, Imperial Coll Wye, Dept Biol, Ashford TN25 5AH, Kent, England
关键词
secondary alcohol dehydrogenase; glycerol dehydrogenase; cold-active enzymes; psychrotolerant bacteria; biotechnology;
D O I
10.1016/S0141-0229(02)00339-3
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A NAD(P)(+)-dependent secondary alcohol dehydrogenase (2degrees ADH) and a NAD(+)-dependent glycerol dehydrogenase (GDH) have been identified in a psychrotolerant Micrococcus sp. and Arthrobacter sp., respectively, both isolated from Antarctic soil. In partially purified cell-free extracts (enriched 84- and 78-fold for 2degrees ADH and GDH, respectively), the enzymes displayed cold activity: the 2degrees ADH had optimum for activity at 33 degreesC and retained 32% of its maximum activity at 6 degreesC, the corresponding values for the GDH were 35 degreesC and 43%. The enzymes were inactivated within 10 min at 50 and 60 degreesC, for 2degrees ADH and GDH, respectively. The 2degrees ADH was active against a wide range of medium chain-length alcohols, preferring (R)-stereoisomers; the enzyme was reversible with a higher affinity for the reduction of ketones. The GDH was active against glycerol and diols containing a secondary alcohol group. These properties make the enzymes candidates for low temperature biotransformations. (C) 2002 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:532 / 538
页数:7
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