BioChem - DOS

His-tagged Horse Liver Alcohol Dehydrogenase: Immobilization and application in the bio-based enantioselective synthesis of (S)-arylpropanols

Process biochemistry

Quaglia, D.; Pori, M.; Galletti, P.; Emer, E.; Paradisi, F.; Giacomini, D.

The novel histidine-tagged Horse Liver Alcohol Dehydrogenase (His-HLADH-EE) was successfully purified and covalently immobilized onto a solid support in a one-step procedure through a metal-directed technique. A full characterization of the immobilized enzyme was carried out. Effects of pH, temperature and organic co-solvents were deeply investigated and they showed a shift in the optimum pH with respect to the free form as well as increased stability to temperature and solvents. The immobilized His-HLADH-EE proved to be effective as catalyst in the reduction of aliphatic and aromatic aldehydes. Application of the free and immobilized His-HLADH-EE to the chemo-enzymatic synthesis of (S)-Profenols demonstrated enhanced enantioselectivity and high reusability of the immobilized form. The achievement of a robust and effective immobilization of an alcohol dehydrogenase substantiated the use of biocatalytic reduction in the synthesis of primary alcohols and valuable chiral intermediates especially for pharmaceutical industries.

2013

Elsevier Applied Science

cc-by-nc-nd

1359-5113

48

5

pp.810-818

10.1016/j.procbio.2013.03.016

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART66085046

Alcohol dehydrogenases; Immobilization; Enantioselective reduction; Profenols; Dynamic kinetic resolution; Horse Liver Alcohol Dehydrogenase