Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Oxidoreductase
Patent
1991-05-06
1993-04-06
Naff, David M.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Oxidoreductase
435853, C12N 904, C12N 100
Patent
active
052003353
ABSTRACT:
A phenylethanol dehydrogenase capable of catalyzing the reduction of acetophenone to R(+)-phenylethanol in the presence of NADPH was isolated from Lactobacilli such as Lactobacillus kefir. The dehydrogenase is also capable of catalyzing the reduction of aromatic, alicyclic and aliphatic ketones selected from the group consisting of p-bromoacetophenone, methylcyclohexanone, acetone, methyl hexyl ketone, 4-phenyl-2-butanone, 1-phenyl-1,2-propanedione, ethyl pentyl ketone, pinacolone, propiophenone and p-chloroacetophenone. The dehydrogenase is rapidly inactivated by EDTA, but conventional inhibitors, chelators and SH-protecting reagents have only a slight effect on activity. The enzyme has a K.sub.M of 6.times.10.sup.-4 M for acetophenone. The dehydrogenase is capable of catalyzing the enzymatic reduction of carbonyl compounds to form optically active hydroxy compounds in the presence of NADPH. In such reactions, NADPH can be simultaneously regenerated in the presence of glucose 6-P and glucose-6-P dehydrogenase or isopropanol.
REFERENCES:
Cripps et al., Eur. J. Biochem., vol. 86, No. 1, 1978, pp. 175-186, abstract.
Murakami Patent Abstracts of Japan, 11(150):C-422, 2597 (May 1987).
Aragozzini et al. "Stereoselective Reduction of Non-Cyclic Carbonyl Compounds by Some Eumycetes", Appl. Microbiol. Biotechnol., 24: 175-177 (1986).
Keinan et al. "Synthetic Applications of Alcohol-Dehydrogenase from Thermoanaerobium Brockii"; Ann. N.Y. Acad. Sci., 501: 130-149 (1987).
Hummel Werner
Kula Maria-Regina
Forschungszentrum Juelich GmbH
Meller Mike
Naff David M.
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