Recombinant expression and biochemical characterization of a novel keratinase BsKER71 from feather degrading bacterium Bacillus subtilis S1-4.

ABSTRACT: Bacillus subtilis S1-4, isolated from chicken feather could efficiently degrade feathers by secreting several extracellular proteases. In order to get insight into the individual protease involved in keratin hydrolysis, a keratinase designed as BsKER71 was cloned and expressed in Bacillus subtilis WB600. In silico analysis revealed that BsKER71 protein contained a mature protein of 36.1 kDa. Further, purified BsKER71 could hydrolyze a variety of natural proteins, such as fibrous protein, collagen protein, casein, keratin and bovine serum albumin. In addition, this keratinase exhibited high enzyme activity in a wide range of pH and optimal pH of 10.0 and 9.0 in the hydrolysis of casein and keratin, respectively. Similarly, the optimal temperature was 55 °C and 50 °C for the hydrolysis of ab

SUBMITTER: Yong B 

PROVIDER: S-EPMC6962420 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature