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Article

Improvement of Trichoderma reesei xylanase II thermal stability by serine to threonine surface mutations.

International journal of biological macromolecules - 1 Jan 2015

Zouari Ayadi Dorra, Hmida Sayari Aida, Ben Hlima Hajer, Ben Mabrouk Sameh, Mezghani Monia, Bejar Samir

Abstract excerpt

Three simple mutants, S80T, S146T, and S149T, and a double mutant, S80T-S149T, were constructed and expressed in Escherichia coli to replace Serine on the surface of the Trichoderma reesei xylanase protein with Threonine residues. While the Wild-type (WT) xylanase showed a half-life time (t1/2) of 20 min at 55 °C, the double mutant was more thermostable exhibiting a t1/2 value of 37 min, followed by the S80T and...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 25158289
DOI: 10.1016/j.ijbiomac.2014.08.014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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