By Overexpression in the Yeast Pichia pastoris to Enhanced Enantioselectivity: New Aspects in the Application of Pig Liver Esterase

Anna Musidlowska; Stefan Lange; Uwe T Bornscheuer

doi:10.1002/1521-3773(20010803)40:15<2851::AID-ANIE2851>3.0.CO;2-V

By Overexpression in the Yeast Pichia pastoris to Enhanced Enantioselectivity: New Aspects in the Application of Pig Liver Esterase

Angew Chem Int Ed Engl. 2001 Aug 3;40(15):2851-2853. doi: 10.1002/1521-3773(20010803)40:15<2851::AID-ANIE2851>3.0.CO;2-V.

Authors

Anna Musidlowska¹, Stefan Lange², Uwe T Bornscheuer¹

Affiliations

¹ Institute of Chemistry and Biochemistry Department of Technical Chemistry and Biotechnology Greifswald University Soldmannstrasse 16, 17487 Greifswald (Germany) Fax: (+49) 3834-86-4373.
² Institute of Technical Biochemistry Stuttgart University (Germany).

PMID: 29712000
DOI: 10.1002/1521-3773(20010803)40:15<2851::AID-ANIE2851>3.0.CO;2-V

Abstract

Stable product quality without the interfering influences of other isoenzymes and hydrolases is possible through the application of recombinant pig liver esterase (rPLE), for which functional expression has now been achieved for the first time. In the hydrolysis of 1-phenyl-2-butyl acetate rPLE leads to substantially higher enantioselectivity than commercial PLE preparations.

Keywords: enzyme catalysis; gene expression; hydrolases; kinetic resolution; pig liver esterase.