Site-directed Mutagenesis of Methionine Residues for Improving the Oxidative Stability of α-amylase from Thermotoga Maritima

Overview

Journal J Biosci Bioeng

Specialties Biochemistry
Biomedical Engineering
Microbiology

Date 2013 May 25

PMID 23702189

Citations 5

Authors

Handan Ozturk

Selin Ece

Ersin Gundeger

Serap Evran

Affiliations

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Abstract

The oxidative stability of α-amylase (AmyC) from Thermotoga maritima was improved by mutating the methionine residues at positions 43 and 44, 55, and 62 to oxidative-resistant alanine residues. The most resistant M55A variant showed 50% residual activity in the presence of 100 mM H₂O₂, whereas the wild-type enzyme was inactive.

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