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Kinetic resolution of diarylmethanols using a mutated variant of lipase CALB
KTH, School of Biotechnology (BIO), Biochemistry.
KTH, School of Biotechnology (BIO), Biochemistry.
2012 (English)In: Tetrahedron, ISSN 0040-4020, E-ISSN 1464-5416, Vol. 68, no 37, 7613-7618 p.Article in journal (Refereed) Published
Abstract [en]

An enzymatic kinetic resolution of diarylmethanols via acylation has been developed. This was achieved by the use of a mutated variant of CALB that accepts larger substrates compared to the wild type. By the use of diarylmethanols with two differently sized aryl groups, enantioselective transformations were achieved. A larger size-difference led to a higher enantioselectivity. In addition, substrates with electronically different aryl groups, such as phenyl and pyridyl, also gave an enantioselective reaction. The highest E value was observed with a substrate where steric and electronic effects were combined.

Place, publisher, year, edition, pages
2012. Vol. 68, no 37, 7613-7618 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-103365DOI: 10.1016/j.tet.2012.06.040ISI: 000307802300013OAI: diva2:560248
Swedish Research CouncilKnut and Alice Wallenberg Foundation

QC 20121012

Available from: 2012-10-12 Created: 2012-10-11 Last updated: 2012-10-12Bibliographically approved

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