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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/51227

Title: A Rigidoporus vinctus alcohol dehydrogenase and its characterization
Authors: Chuian‐Fu Ken
Shiun‐Jye Tzeng
Lisa Wen
Chi‐Tsai Lin
Contributors: 國立臺灣海洋大學:生命科學暨生物科技學系
Date: 2016-01
Issue Date: 2018-11-19T08:00:07Z
Publisher: Journal of the Chinese Chemical Society
Abstract: Abstract: Alcohol dehydrogenases (ADHs; E.C. are widely distributed enzymes found in many microorganisms. ADHs are oxidoreductases that catalyze the NAD(P)+‐dependent conversion of alcohols to aldehydes or ketones as well as the reverse reaction. The ADH cloned from Rigidoporus vinctus (RvADH) was 1035 bp that encodes a protein of 344 amino acid residues with calculated molecular mass of 38.39 kDa. This ADH is belonging to the medium‐chain family (medium‐chain dehydrogenase/reductase (MDR) and has the highly conserved GXXGXXG sequence found in the MDR family which found as the coenzyme‐binding pocket. To characterize the ADH protein, the coding region was subcloned into an expression vector pET‐20b(+) and transformed into E. coli Rosetta (DE3). The recombinant His6‐tagged ADH was overexpressed and purified by Ni2+‐nitrilotriacetic acid Sepharose. The purified enzyme showed one band on 12 % sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. The Michaelis constant (KM) value of the recombinant enzyme for ethanol was 0.79 mM. In substrates specificity analysis showed that RvADH had great oxidative activity toward primary alcohols. However, the less activtiy toward secondary alcohols and alcohol derivatives were compared with ethanol. Regarding the reductase activity showed low or even no activity to aldehydes and ketone.
Relation: 63(3) pp.308-312
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/51227
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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