Activity of Lactobacillus brevis alcohol dehydrogenase on primary and secondary alcohol biofuel precursors

Ibrahim Halloum, Brian Thompson, Shawn Pugh, David Nielsen

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)24-37
Number of pages14
JournalFermentation
Volume1
Issue number1
DOIs
StatePublished - Dec 1 2015

Keywords

  • Alcohol dehydrogenase
  • Biofuel
  • Butanol
  • Lactobacillus brevis

ASJC Scopus subject areas

  • Plant Science
  • Food Science
  • Biochemistry, Genetics and Molecular Biology (miscellaneous)

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