Open AccessStreptomyces sp. K47 alkaline proteases: partial purification and analysis by zymography
Author(s) -
Cengiz Çorbacı,
Kadriye Özcan
Publication year - 2021
Publication title -
acta scientiarum. technology/acta scientiarum. technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.183
H-Index - 17
eISSN - 1807-8664
pISSN - 1806-2563
DOI - 10.4025/actascitechnol.v43i1.51486
Subject(s) - proteases , zymography , enzyme , chemistry , streptomyces , chromatography , yeast extract , protease , incubation , pmsf , yeast , biochemistry , biology , fermentation , bacteria , genetics
Microbial enzymes are used as organic catalysts in different industrial processes. In this study, we aimed to produce and investigate alkaline proteases from a novel actinobacterium strain isolated from a Black Sea marine sediment. The optimal production conditions for Streptomyces sp. K47 alkaline proteases was 4-days incubation at 28ºC in a salt-free medium buffered with 50 mM Tris-HCl buffer (pH 9.0) and containing glucose (1.0%, w v-1) and yeast extract (0.5%, w v-1). The enzyme solution was partially purified using (NH4)2SO4 precipitation (40-70%). After desalting, it was purified 1-84 fold with a recovery of 19.42%. Zymogram analyses revealed the presence of more than one protease enzyme. The enzyme solution exhibited maximum activity at pH 9.0 and 37ºC, remaining stable after a 2-hour incubation at all tested conditions. Streptomyces sp. K47 has the potential to be used in industrial processes because of its ability to produce multiple protease enzymes displaying stability in a broad pH and temperature range.