Description

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

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.

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    Date Created
    • 2015-08-05
    Resource Type
  • Text
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    Identifier
    • Digital object identifier: 10.3390/fermentation1010024
    • Identifier Type
      International standard serial number
      Identifier Value
      2311-5637

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    Halloum, I., Thompson, B., Pugh, S., & Nielsen, D. (2015). Activity of Lactobacillus brevis Alcohol Dehydrogenase on Primary and Secondary Alcohol Biofuel Precursors. Fermentation, 1(1), 24-37. doi:10.3390/fermentation1010024

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