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Co-Immobilization of ADH and GDH on Metal-Organic-Framework: An Effective Biocatalyst for Asymmetric Reduction of Ketones.
- Source :
-
Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Jun 17; Vol. 25 (12), pp. e202400147. Date of Electronic Publication: 2024 May 21. - Publication Year :
- 2024
-
Abstract
- Chiral alcohols are not only important building blocks of various bioactive natural compounds and pharmaceuticals, but can serve as synthetic precursors for other valuable organic chemicals, thus the synthesis of these products is of great importance. Bio-catalysis represents one effective way to obtain these molecules, however, the weak stability and high cost of enzymes often hinder its broad application. In this work, we designed a biological nanoreactor by embedding alcohol dehydrogenase (ADH) and glucose dehydrogenase (GDH) in metal-organic-framework ZIF-8. The biocatalyst ADH&GDH@ZIF-8 could be applied to the asymmetric reduction of a series of ketones to give chiral alcohols in high yields (up to 99 %) and with excellent enantioselectivities (>99 %). In addition, the heterogeneous biocatalyst could be recycled and reused at least four times with slight activity decline. Moreover, E. coli containing ADH and GDH was immobilized by ZIF-8 to form biocatalyst E. coli@ZIF-8, which also exhibits good catalytic behaviours. Finally, the chiral alcohols are further converted to marketed drugs (R)-Fendiline, (S)-Rivastigmine and NPS R-568 respectively.<br /> (© 2024 Wiley-VCH GmbH.)
- Subjects :
- Oxidation-Reduction
Stereoisomerism
Alcohol Dehydrogenase metabolism
Alcohol Dehydrogenase chemistry
Metal-Organic Frameworks chemistry
Metal-Organic Frameworks metabolism
Ketones chemistry
Ketones metabolism
Enzymes, Immobilized metabolism
Enzymes, Immobilized chemistry
Biocatalysis
Escherichia coli enzymology
Escherichia coli metabolism
Glucose 1-Dehydrogenase metabolism
Glucose 1-Dehydrogenase chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1439-7633
- Volume :
- 25
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Chembiochem : a European journal of chemical biology
- Publication Type :
- Academic Journal
- Accession number :
- 38629211
- Full Text :
- https://doi.org/10.1002/cbic.202400147