Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.

The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation.

Regulating acidogenesis and methanogenesis for the separated bio-generation of hydrogen and methane from saline-to-hypersaline industrial wastewater.

Given the limitations of acidogens and methanogens activities under saline environments, this work aims to optimize the main operational parameters affecting hydrogen and methane production from saline-to-hypersaline wastewater containing mono-ethylene glycol (MEG). MEG is the main contaminant in several saline industrial effluents. Anaerobic baffled reactor (ABR), as a multi-stage system, was used at different temperatures (i.

Increase in the thermostability of GH11 xylanase XynJ from Bacillus sp. strain 41M-1 using site saturation mutagenesis.

GH11 xylanase XynJ from Bacillus sp. strain 41M-1 has a β-jellyroll fold composed of eight β strands with a deep active-site cleft. We hypothesized that the thermostability of XynJ will increase if the flexibility of the β strands in the jellyroll structure is decreased without impairing activity.

Increase in the thermostability of Bacillus sp. strain TAR-1 xylanase using a site saturation mutagenesis library.

Unlabelled: Site saturation mutagenesis library is a recently developed technique, in which any one out of all amino acid residues in a target region is substituted into other 19 amino acid residues. In this study, we used this technique to increase the thermostability of a GH10 xylanase, XynR, from Bacillus sp. strain TAR-1.