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Article

Selection of horseradish peroxidase variants with enhanced enantioselectivity by yeast surface display.

Chemistry & biology - 1 Oct 2007

Lipovsek Dasa, Antipov Eugene, Armstrong Kathryn A, Olsen Mark J, Klibanov Alexander M, Tidor Bruce, Wittrup K Dane

Abstract excerpt

We report a method for in vitro selection of catalytically active enzymes from large libraries of variants displayed on the surface of the yeast S. cerevisiae. Two libraries, each containing approximately 2 x 10(6) variants of horseradish peroxidase (HRP), were constructed; one involved error-prone PCR that sampled mutations throughout the coding sequence, whereas the other involved complete combinatorial...

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PMID: 17961829
DOI: 10.1016/j.chembiol.2007.09.008

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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