Site-directed mutagenesis of methionine residues for improving the oxidative stability of α-amylase from Thermotoga maritima
Articles > Article · 2013
Authors: Handan OZTURK, Selin ECE, Ersin GUNDEGER, Serap EVRAN
Journal of Bioscience and Bioengineering, Journal Indexed in SCI Expanded, International, WoS, 2013, vol 116, pp 449-451
DOI: 10.1016/j.jbiosc.2013.04.018
Summary
The oxidative stability of alpha-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. (C) 2013, The Society for Biotechnology, Japan. All rights reserved.