Production and purification of novel thermostable alkaline protease from Anoxybacillus sp. KP1
dc.contributor.author | Bekler, Fatma Matpan | |
dc.contributor.author | Acer, Ömer | |
dc.contributor.author | Güven, Kemal | |
dc.date.accessioned | 2024-04-24T17:56:41Z | |
dc.date.available | 2024-04-24T17:56:41Z | |
dc.date.issued | 2015 | |
dc.department | Dicle Üniversitesi, Fen Fakültesi, Biyoloji Bölümü | en_US |
dc.description.abstract | 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%. | en_US |
dc.identifier.citation | 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. | |
dc.identifier.doi | 10.14715/cmb/2015.61.4.18 | |
dc.identifier.endpage | 120 | en_US |
dc.identifier.issn | 0145-5680 | |
dc.identifier.issue | 4 | en_US |
dc.identifier.pmid | 26429301 | |
dc.identifier.scopus | 2-s2.0-84963647533 | |
dc.identifier.scopusquality | Q4 | |
dc.identifier.startpage | 113 | en_US |
dc.identifier.uri | https://doi.org/10.14715/cmb/2015.61.4.18 | |
dc.identifier.uri | https://hdl.handle.net/11468/23622 | |
dc.identifier.volume | 61 | en_US |
dc.indekslendigikaynak | Scopus | |
dc.indekslendigikaynak | PubMed | |
dc.language.iso | en | en_US |
dc.publisher | Cellular and Molecular Biology Association | en_US |
dc.relation.ispartof | Cellular and Molecular Biology | |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/closedAccess | en_US |
dc.subject | Anoxybacillus | en_US |
dc.subject | Production | en_US |
dc.subject | Protease | en_US |
dc.subject | Purification | en_US |
dc.subject | Thermophiles | en_US |
dc.title | Production and purification of novel thermostable alkaline protease from Anoxybacillus sp. KP1 | en_US |
dc.title | Production and purification of novel thermostable alkaline protease from Anoxybacillus sp. KP1 | |
dc.type | Article | en_US |