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Review article

Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations

S. Leuchs ; DECHEMA Karl-Winnacker-Institut, Frankfurt am Main, Germany
L. Greiner ; DECHEMA Karl-Winnacker-Institut, Frankfurt am Main, Germany; Institut für Technische und Makromolekulare Chemie, RWTH Aachen University, Aachen, Germany

Fulltext: english, pdf (723 KB) pages 267-281 downloads: 1.635* cite
APA 6th Edition
Leuchs, S. & Greiner, L. (2011). Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations. Chemical and Biochemical Engineering Quarterly, 25 (2), 267-281. Retrieved from https://hrcak.srce.hr/69863
MLA 8th Edition
Leuchs, S. and L. Greiner. "Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations." Chemical and Biochemical Engineering Quarterly, vol. 25, no. 2, 2011, pp. 267-281. https://hrcak.srce.hr/69863. Accessed 18 May 2021.
Chicago 17th Edition
Leuchs, S. and L. Greiner. "Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations." Chemical and Biochemical Engineering Quarterly 25, no. 2 (2011): 267-281. https://hrcak.srce.hr/69863
Harvard
Leuchs, S., and Greiner, L. (2011). 'Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations', Chemical and Biochemical Engineering Quarterly, 25(2), pp. 267-281. Available at: https://hrcak.srce.hr/69863 (Accessed 18 May 2021)
Vancouver
Leuchs S, Greiner L. Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations. Chemical and Biochemical Engineering Quarterly [Internet]. 2011 [cited 2021 May 18];25(2):267-281. Available from: https://hrcak.srce.hr/69863
IEEE
S. Leuchs and L. Greiner, "Alcohol Dehydrogenase from Lactobacillus brevis: A Versatile Robust Catalyst for Enantioselective Transformations", Chemical and Biochemical Engineering Quarterly, vol.25, no. 2, pp. 267-281, 2011. [Online]. Available: https://hrcak.srce.hr/69863. [Accessed: 18 May 2021]

Abstracts
The alcohol dehydrogenase from Lactobacillus brevis (LbADH) is a versatile catalyst for enantioselective reduction of ketones. Its substrate scope is wide with high regio- and enantioselectivity. In this critical review, we have gathered the information available on the substrate scope as well as the applications reported. Quantitative information such
as productivity per catalyst, space-time yield (STY), cofactor utilisation, and stability are derived to allow comparison and assessment of practical value.

Keywords
Biocatalysis; alcohol dehydrogenase; Lactobacillus brevis; critical review; application

Hrčak ID: 69863

URI
https://hrcak.srce.hr/69863

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