Akademik Veri Yönetim Sistemi
European Biotechnology Congress 2021, Sofija, Bulgaristan, 23 - 25 Eylül 2021, ss.86, (Özet Bildiri)
Keratinases from microorganisms have obtained a great deal of attention in the recent years particularly due to their multitude of biotechnological
applications. An extremely alkaliphilic bacterial strain, Bacillus sp. was isolated from salt lake in Turkey. According to morfological and
biochemical tests the isolated strain identified as Bacillus sp and called Bacillus sp. SK-31.
The partially purified enzyme displayed maximum activity at pH 10.0 and 130°C. Bacillus sp. The enzyme showed an average of 58% activity at
20-110°C, 87% at 120-150°C, and 114% at 20-90°C, respectively.
The enzyme retained 98% of its original activity at pH 6.0-11.0 and 91% at pH 6.0-13.0. The partially purified keratinase enzyme was stable
at 3-30% NaCl concentrations and preserved its original activity by 101%. Enzyme retained its activity in the presence of EDTA, SDS, PMSF,
β-mercaptoethanol, CaCl2 and H2O2 up to %92,%103, %103, %103, %93 and %102 respectively.
TLC analyses of the hydrolysate of feather keratin revealed the presence of histidine, glysine, proline, sistin, tyrozin, and etc. The results of this
study showes that the enzyme is active in extrem temperature, wide pH range and NaCl concentration. Consequently the enzyme can applicable
detergent, fertilizers, cosmetics, feed additive and dehairing areas.