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Suppression of Water as a Nucleophile in Candida antarctica Lipase B Catalysis
KTH, School of Biotechnology (BIO), Biochemistry.
KTH, School of Biotechnology (BIO), Biochemistry.
KTH, School of Biotechnology (BIO), Biochemistry.ORCID iD: 0000-0002-2993-9375
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2010 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 11, no 6, 796-801 p.Article in journal (Refereed) Published
Abstract [en]

A water tunnel in Candida antarctica lipase B that provides the active site with substrate water is hypothesized. A small, focused library created in order to prevent water from entering the active site through the tunnel was screened for increased transacylation over hydrolysis activity. A single mutant, S47L, in which the inner part of the tunnel was blocked, catalysed the transacylation of vinyl butyrate to 20 mm butanol 14 times faster than hydrolysis. The single mutant Q46A, which has a more open outer end of the tunnel, showed an increased hydrolysis rate and a decreased hydrolysis to transacylation ratio compared to the wild-type lipase. Mutants with a blocked, tunnel could be very useful in applications in which hydrolysis is unwanted, such as the acylation of highly hydrophilic compounds in the presence of water.

Place, publisher, year, edition, pages
2010. Vol. 11, no 6, 796-801 p.
Keyword [en]
Candida antarctica lipase B, hydrolysis, library screening, mutagenesis, rational design, transacylation
National Category
Biochemistry and Molecular Biology Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-27912DOI: 10.1002/cbic.200900743ISI: 000277299800012OAI: oai:DiVA.org:kth-27912DiVA: diva2:383047
Note
QC 20110104Available from: 2011-01-04 Created: 2011-01-03 Last updated: 2017-12-11Bibliographically approved

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Martinelle, Mats

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