源于同化2-苯乙醇的短杆菌属菌株KU 1309的具有广泛底物特异性的乙醇脱氢酶的纯化与特性分析
Purification and characterization of the alcohol dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU 1309.
作者信息
Hirano Jun-ichiro, Miyamoto Kenji, Ohta Hiromichi
机构信息
Department of Biosciences and Informatics, Center for Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Yokohama 223-8522, Japan.
出版信息
J Biosci Bioeng. 2005 Sep;100(3):318-22. doi: 10.1263/jbb.100.318.
A novel 2-phenylethanol dehydrogenase has been purified from a soil bacterium Brevibacterium sp. KU 1309. The enzyme was purified about 1400-fold to homogeneity, and found to be a monomeric enzyme of apparent 39 kDa. The enzyme had broad substrate specificity and catalyzes a reversible oxidation of various primary alcohols to aldehydes. The enzyme required NAD+, but not NADP+ as a cofactor. Thus, the enzyme was classified into a group of NAD+-dependent primary alcohol dehydrogenase. The activity was inhibited by Cu2+, Ni2+, Ba2+, Hg2+ and p-chloromercuribenzoate. The enzyme is expected to be applicable as an effective biocatalyst in the oxidation of various alcohols.
一种新型的2-苯乙醇脱氢酶已从土壤细菌短杆菌属菌株KU 1309中纯化出来。该酶被纯化至约1400倍的纯度且达到均一性，发现它是一种表观分子量为39 kDa的单体酶。该酶具有广泛的底物特异性，可催化各种伯醇可逆氧化为醛。该酶需要NAD⁺作为辅因子，而不需要NADP⁺。因此，该酶被归类为NAD⁺依赖性伯醇脱氢酶。其活性受到Cu²⁺、Ni²⁺、Ba²⁺、Hg²⁺和对氯汞苯甲酸的抑制。预计该酶可作为各种醇氧化的有效生物催化剂。
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