Bekler, Fatma MatpanAcer, ÖmerGüven, Kemal2024-04-242024-04-242015Bekler, 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), 113-120.0145-5680https://doi.org/10.14715/cmb/2015.61.4.18https://hdl.handle.net/11468/23622In 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%.eninfo:eu-repo/semantics/closedAccessAnoxybacillusProductionProteasePurificationThermophilesArticle6141131202-s2.0-849636475332642930110.14715/cmb/2015.61.4.18Q4