Activity of Lactobacillus brevis Alcohol Dehydrogenase on Primary and Secondary Alcohol Biofuel Precursors
| Autor: | Brian Thompson, David R. Nielsen, Ibrahim Halloum, Shawn Pugh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
chemistry.chemical_classification
biology Sequence analysis Lactobacillus brevis Butanol alcohol dehydrogenase Substrate (chemistry) Alcohol Plant Science biology.organism_classification Biochemistry Genetics and Molecular Biology (miscellaneous) Aldehyde butanol chemistry.chemical_compound Enzyme chemistry Biochemistry biology.protein biofuel Food Science Alcohol dehydrogenase |
| Zdroj: | Fermentation Volume 1 Issue 1 Pages 24-37 |
| ISSN: | 2311-5637 |
| DOI: | 10.3390/fermentation1010024 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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