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Mutant Lipase-Catalyzed Kinetic Resolution of Bulky Phenyl Alkyl sec-Alcohols: A Thermodynamic Analysis of Enantioselectivity
KTH, School of Biotechnology (BIO), Biochemistry.
KTH, School of Biotechnology (BIO), Biochemistry.ORCID iD: 0000-0002-4066-2776
KTH, School of Biotechnology (BIO), Biochemistry.
2010 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 11, no 3, 411-416 p.Article in journal (Refereed) Published
Abstract [en]

The size of the stereoselectivity pocket of Candida antarctica lipase B limits the range of alcohols that can be resolved with this enzyme. These steric constrains have been changed by increasing the size of the pocket by the mutation W104A. The mutated enzyme has good activity and enantioselectivity toward bulky secondary alcohols, such as 1-phenylalkanols, with alkyl chains up to eight carbon atoms. The S enantiomer was preferred in contrast to the wild-type enzyme, which has R selectivity. The magnitude of the enantioselectivity changes in an interesting way with the chain length of the alkyl moiety. It is governed by interplay between entropic and enthalpic contributions and substrates with long alkyl chains are resolved best with E values higher than 100. The enantioselectivity increases with temperature for the small substrates, but decreases for the long ones.

Place, publisher, year, edition, pages
2010. Vol. 11, no 3, 411-416 p.
Keyword [en]
enantioselectivity, enzyme catalysis, lipases, thermodynamics, active-site titration, candida-antarctica, secondary alcohols, rational, redesign, reacts faster, temperature, transesterification, stereochemistry, entropy, water
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-19267DOI: 10.1002/cbic.200900635ISI: 000275039500018Scopus ID: 2-s2.0-76649139801OAI: oai:DiVA.org:kth-19267DiVA: diva2:337314
Funder
Swedish Research Council
Note
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved

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Syrén, Per-Olof

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