Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Combinatorial Library Based Engineering of Candida antarctica Lipase A for Enantioselective Transacylation of sec-Alcohols in Organic Solvent
KTH, School of Biotechnology (BIO), Industrial Biotechnology. Stockholm University, Sweden . (Albanova University Center)ORCID iD: 0000-0003-2371-8755
2015 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 54, no 14, 4284-4288 p.Article in journal (Refereed) Published
Abstract [en]

A method for determining lipase enantioselectivity in the transacylation of sec-alcohols in organic solvent was developed. The method was applied to a model library of Candida antarctica lipase A (CalA) variants for improved enantioselectivity (E values) in the kinetic resolution of 1-phenylethanol in isooctane. A focused combinatorial gene library simultaneously targeting seven positions in the enzyme active site was designed. Enzyme variants were immobilized on nickel-coated 96-well microtiter plates through a histidine tag (His(6)-tag), screened for transacylation of 1-phenylethanol in isooctane, and analyzed by GC. The highest enantioselectivity was shown by the double mutant Y93L/L367I. This enzyme variant gave an E value of 100 (R), which is a dramatic improvement on the wild-type CalA (E=3). This variant also showed high to excellent enantioselectivity for other secondary alcohols tested.

Place, publisher, year, edition, pages
2015. Vol. 54, no 14, 4284-4288 p.
Keyword [en]
biocatalysis, kinetic resolution, lipase A, protein engineering, secondary alcohols
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kth:diva-165210DOI: 10.1002/anie.201410675ISI: 000351679600024PubMedID: 25676632Scopus ID: 2-s2.0-84925582964OAI: oai:DiVA.org:kth-165210DiVA: diva2:810384
Note

QC 20150507

Available from: 2015-05-07 Created: 2015-04-24 Last updated: 2017-12-04Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedScopus

Authority records BETA

Humble, Maria Svedendahl

Search in DiVA

By author/editor
Humble, Maria Svedendahl
By organisation
Industrial Biotechnology
In the same journal
Angewandte Chemie International Edition
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 42 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf