Site-directed mutagenesis of methionine residues for improving the oxidative stability of alpha-amylase from Thermotoga maritima
Küçük Resim Yok
Tarih
2013
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Soc Bioscience Bioengineering Japan
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
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.
Açıklama
Anahtar Kelimeler
alpha-Amylase, Thermotoga maritima, Oxidative stability, Protein engineering, Site-directed mutagenesis of methionine
Kaynak
Journal of Bioscience and Bioengineering
WoS Q Değeri
Q2
Scopus Q Değeri
Cilt
116
Sayı
4
