Site-directed mutagenesis of methionine residues for improving the oxidative stability of ?-amylase from Thermotoga maritima
Küçük Resim Yok
Tarih
2013
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
The oxidative stability of ?-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 100mM H2O2, whereas the wild-type enzyme was inactive. © 2013 The Society for Biotechnology, Japan.
Açıklama
Anahtar Kelimeler
?-Amylase, Oxidative stability, Protein engineering, Site-directed mutagenesis of methionine, Thermotoga maritima
Kaynak
Journal of Bioscience and Bioengineering
WoS Q Değeri
Scopus Q Değeri
Q2
Cilt
116
Sayı
4
