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Article

Engineering highly thermostable xylanase variants using an enhanced combinatorial library method.

Protein engineering, design & selection : PEDS - 1 Aug 2011

Hokanson Craig A, Cappuccilli Guido, Odineca Tatjana, Bozic Marino, Behnke Craig A, Mendez Michael, Coleman William J, Crea Roberto

Abstract excerpt

A new directed evolution method was used to enhance the thermostability of the wild-type GH11 xylanase 2 (known as BD-11) from Hypocrea jecorina (Trichoderma reesei). Both Look-Through Mutagenesis (LTM™), which is a method for rapidly screening selected positions in the protein sequence for amino acids that introduce favorable properties, and Combinatorial Beneficial Mutagenesis (CBM™), which is a method for...

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PMID: 21708791
DOI: 10.1093/protein/gzr028

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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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