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Published on: October 2, 2012
A short-chain dehydrogenase plays a key role in cellulosic D-lactic acid fermentability of Pediococcus acidilactici
Zhongyang Qiu1, Chun Fang2, Qiuqiang Gao2
1State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, China; Jiangsu Key Laboratory for Biomass-based Energy and Enzyme Technology, Huaiyin Normal University, 111 West Changjiang Road, Huaian 223300, Jiangsu, China.
Abstract:
Phenolic aldehydes from lignocellulose pretreatment are strong inhibitors of cell growth and metabolism of cellulosic lactic acid bacteria. Their low solubility and recalcitrance highly reduce the removal efficiency of various detoxification methods. This study shows a simultaneous conversion of phenolic aldehydes and fermentation of D-lactic acid by Pediococcus acidilactici using corn stover feedstock. Vanillin was found to be the strongest phenolic aldehyde inhibitor to P. acidilactici. The overexpression of a short-chain dehydrogenase encoded by the gene CGS9114_RS09725 from Corynebacterium glutamicum was identified to play a key role in D-lactic acid fermentability of P. acidilactici. The engineered P. acidilactici with the genome integration of CGS9114_RS09725 showed the accelerated vanillin reduction and improved cellulosic D-lactic acid production. This study reveals that vanillin conversion is crucial for D-lactic acid fermentation, and the direct expression of a specific vanillin reduction gene in lactic acid bacterium efficiently improves cellulosic D-lactic acid production.
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