Site-directed mutagenesis of methionine residues for improving the oxidative stability of alpha-amylase from Thermotoga maritima


OZTURK H., ECE S., GUNDEGER E., EVRAN S.

JOURNAL OF BIOSCIENCE AND BIOENGINEERING, vol.116, no.4, pp.449-451, 2013 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 116 Issue: 4
  • Publication Date: 2013
  • Doi Number: 10.1016/j.jbiosc.2013.04.018
  • Title of Journal : JOURNAL OF BIOSCIENCE AND BIOENGINEERING
  • Page Numbers: pp.449-451
  • Keywords: alpha-Amylase, Thermotoga maritima, Oxidative stability, Protein engineering, Site-directed mutagenesis of methionine, HYDROGEN-PEROXIDE, RESISTANCE, REPLACEMENT, ENZYMES

Abstract

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.