Biochemical Characterization of Recombinant Thermostable Cohnella sp. A01 β-Glucanase

ABSTRACT: Background:Typically, non-cellulytic glucanase, including fungi and yeast cell wall hydrolyzing enzymes, are released by some symbiotic fungi and plants during the mycoparasitic fungi attack on plants. These enzymes are known as the defense mechanisms of plants. This study intends to investigate the biochemical properties of β-1,6-glucanase (bg16M) from native thermophilic bacteria, Cohnella A01. Methods:bg16M gene was cloned and expressed in E. coli BL21 (DE3). The enzyme was purified utilizing Ni-NTA nikcle sepharose column. Pustulan and laminarin were selected as substrates in enzyme assay. The purified bg16M enzyme was treated with different pH, temperature, metal ions, and detergents. Results:The expressed protein, including 639 amino acids, showed a high similarity with the hydrolyti

SUBMITTER: Rezaie M 

PROVIDER: S-EPMC6058188 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature