Characterization of an acetoin reductase/2,3-butanediol dehydrogenase from Clostridium ljungdahlii DSM 13528.
作者： Yang Tan , Zi-Yong Liu , Zhen Liu , Fu-Li Li
DOI: 10.1016/J.ENZMICTEC.2015.06.011
关键词: Alcohol dehydrogenase 、 Biochemistry 、 2,3-Butanediol 、 Clostridium acetobutylicum 、 Acetoin 、 Clostridium 、 Dehydrogenase 、 Metabolic engineering 、 Clostridium ljungdahlii 、 Biology
摘要: Acetoin reductase catalyzes the formation of 2,3-butanediol from acetoin. In Clostridium ljungdahlii DSM 13528, gene CLJU_c23220 encoding putative Zn(2+)-dependent alcohol dehydrogenase was cloned and expressed in Escherichia coli. The recombinant enzyme, CLAR, can catalyze conversion acetoin to with NADPH as cofactor. Furthermore, introduced into acetobutylicum ATCC 824 transformant conferred capacity production. batch fermentation produced up 3.1g/L 2,3-butanediol, well acetone, butanol ethanol (ABE, 17.8 g/L) amounts similar those by wild type strain. This study provides conclusive evidence at protein level that is key responsible for C. 13528. Moreover, modified via one-step metabolic engineering produce without influencing ABE
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