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Novel biocatalyst for the asymmetric reduction of ketones : Permeabilized cells of Gluconobacter oxydans

Adlercreutz, Patrick (author)
Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
 (creator_code:org_t)
Elsevier BV, 1991
1991
English 6 s.
In: Enzyme and Microbial Technology. - : Elsevier BV. - 0141-0229. ; 13:1, s. 9-14
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Gluconobacter oxydans (ATCC 621) were permeabilized with toluene and then lyophilized. This crude enzyme preparation was used to reduce eleven ketones to (S)-alcohols with high enantiomeric excess (for most alcohols 93%-99% e.e.). The coenzyme NADH was regenerated either by adding a second enzyme, formate dehydrogenase, and its substrate, formate, or with 2-butanol as a second substrate for the G. oxydans enzyme(s). With the first of these methods, almost complete conversion was achieved. Permeabilized cells immobilized in calcium alginate gel were used for 18 days without any significant loss of catalytic activity.

Subject headings

TEKNIK OCH TEKNOLOGIER  -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
ENGINEERING AND TECHNOLOGY  -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)

Keyword

alcohol dehydrogenase
asymmetric reduction
Gluconobacter oxydans

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art (subject category)
ref (subject category)

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