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Article

A single residual replacement improves the folding and stability of recombinant cassava hydroxynitrile lyase in E. coil.

Biotechnology letters - 1 Jul 2003

Yan Gonghong, Cheng Shuhua, Zhao Guogang, Wu Sheng, Liu Yanbing, Sun Wanru

Abstract excerpt

Substitution of Ser113 for Gly113 in the cap domain of hydroxynitrile lyase from Manihot esculenta (MeHNL) was performed by site-directed mutagenesis to improve its self-generated folding and stability under denaturation conditions. The yield of the recombinant mutant HNL1 (mut-HNL1), which had higher specific activity than the wild type HNL0 (wt-HNL0), was increased by 2 to 3-fold. Thermostability of MeHNL was...

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Identifiers

PMID: 12889812
DOI: 10.1023/a:1024182228057

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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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