An extreme halophilic xylanase from camel rumen metagenome with elevated catalytic activity in high salt concentrations.

ABSTRACT: An extreme halophilic xylanase, designated as XylCMS, was characterized by cloning and expression of the encoding gene from a camel rumen metagenome. XylCMS proved to be a GH11 xylanase with high identity to a hypothetical glycosyl hydrolase from Ruminococcus flavefaciens. XylCMS with a molecular weight of about 47 kDa showed maximum activity at pH 6 and 55 °C. The enzyme activity was significantly stimulated by NaCl in 1-5 M concentrations. Interestingly, the optimum temperature was not influenced by NaCl but the K_cat of the enzyme was enhanced by 2.7-folds at 37 °C and 1.2-folds at 55 °C. The K_m value was decreased with NaCl by 4.3-folds at 37 °C and 3.7-folds at 55 °C resulting in a significant increase in catalytic efficiency (K_cat/K_m) by 11.

SUBMITTER: Ghadikolaei KK 

PROVIDER: S-EPMC6579805 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature