Production and purification of novel thermostable alkaline protease from Anoxybacillus sp. KP1
[ X ]
Tarih
2015
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Cellular and Molecular Biology Association
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
In this study, an extracellular novel alkaline protease (EC 3.4.21-24, 99) from a thermophilic and aerobic strain of Anoxybacillus sp. KP1 has been studied. Maximum protease activity was obtained at 50 °C at pH 9.0 after 24 hours of incubation. Among the carbon and nitrogen sources used; the optimum protease production was with soluble starch, maltose, urea and casamino acid. The enzyme was purified by ammonium sulphate precipitation and Sephadex G-75 gel chromatography. Molecular weight of purified enzyme was determined as 106 kDa by SDS-PAGE. Purified protease was stable at 50-60 °C and at pH 9.0 for 1 h. The enzyme activity was increased in the presence of Ca2+, Cu2+, Tween 80 and Triton X-100, however the enzyme activity was inhibited in the presence of Hg2+, ethylene diamine tetra acetic acid (EDTA) and H2O2. Proteolytic activity was completely inhibited by phenyl methyl sulfonyl fluoride (PMSF). The enzyme seems to be a serine alkaline protease. In the presence of detergents, the protease was clearly stable and residual activity was between 73-82%.
Açıklama
Anahtar Kelimeler
Anoxybacillus, Production, Protease, Purification, Thermophiles
Kaynak
Cellular and Molecular Biology
WoS Q Değeri
Scopus Q Değeri
Q4
Cilt
61
Sayı
4
Künye
Bekler, F. M., Acer, Ö. ve Güven, K. (2015). Production and purification of novel thermostable alkaline protease from Anoxybacillus sp. KP1. Cellular and Molecular Biology, 61(4), 113-120.
