Activity of Lactobacillus brevis Alcohol Dehydrogenase on Primary and Secondary Alcohol Biofuel Precursors

Fermentation

Ibrahim Halloum²  Brian Thompson²  Shawn Pugh²  David R. Nielsen¹ 

[1] Chemical Engineering, School for Engineering of Matter, Transport and Energy, Arizona State University, P.O. Box 876106, Tempe, AZ 85287-6106, USA;

关键词: alcohol dehydrogenase;    Lactobacillus brevis;    butanol;    biofuel;   

DOI  :  10.3390/fermentation1010024

来源: mdpi

【 摘 要 】

The R-specific alcohol dehydrogenase (ADH) from Lactobacillus brevis LB19 (LbADH) was studied with respect to its ability to reduce a series of 3- through 5-carbon 2-alkanones and aldehydes of relevance as biofuel precursors. Although active on all substrates tested, LbADH displays a marked preference for longer chain substrates. Interestingly, however, 2-alkanones were found to impose substrate inhibition towards LbADH, whereas aldehyde substrates rendered no such effect. Inhibition caused by 2-alkanones was furthermore found to intensify with increasing chain length. Despite demonstrating both primary and secondary ADH activities, a preliminary sequence analysis suggests that LbADH remains distinct from other, previously characterized primary-secondary ADHs. In addition to further characterizing the substrate range of this industrially important enzyme, this study suggests that LbADH has the potential to serve as a useful enzyme for the engineering of various novel alcohol biofuel pathways.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.