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Article

The effect of thermostabilising mutations on the pressure stability of Trichoderma reesei GH11 xylanase.

Protein engineering, design & selection : PEDS - 1 Dec 2012

Li H, Murtomäki L, Leisola M, Turunen O

Abstract excerpt

We studied the pressure stability of disulphide bridge mutants of Trichoderma reesei XYNII at 500-5000 bar. The inactivation of XYNII and its mutants was strongest above 4000 bar. The pressure stability correlated with the thermostability order of the XYNII mutants, indicating that the stabilising mutations in protein regions important for thermostability also protect the enzyme at high pressure. In combination...

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Identifiers

PMID: 22942394
DOI: 10.1093/protein/gzs052

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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