Simultaneous enhancement of activity and stability of Bacillus safensis-derived laccase and its application in lignocellulose saccharification.

Effective hydrolysis of lignocelluloses for producing reducing sugar is impeded by the covalent binding of hemicellulose and cellulose through lignin, which could be eliminated by laccases. This study identified a novel thermostable laccase from Bacillus safensis TCCC 111022 and created an iterative mutant E231D/Y441H, exhibiting 1.59-fold greater specific activity and a 183 % greater half-life at 80°C than the wild-type enzyme.

High-level production of xylose from agricultural wastes using GH11 endo-xylanase and GH43 β-xylosidase from Bacillus sp.

As a promising feedstock, alkali-extracted xylan from lignocellulosic biomass is desired for producing xylose, which can be used for renewable biofuels production. In this study, an efficient pathway has been established for low-cost and high-yield production of xylose by hydrolysis of alkali-extracted xylan from agricultural wastes using an endo-1,4-xylanase (XYLA) from Bacillus safensis TCCC 111022 and a β-xylosidase (XYLO) from B. pumilus TCCC 11573.

Insights into the mechanism for the high-alkaline activity of a novel GH43 β-xylosidase from Bacillus clausii with a promising application to produce xylose.

Nowadays, alkali-tolerant β-xylosidases and their molecular mechanism of pH adaptability have been poorly studied. Here, a novel GH43 β-xylosidase (XYLO) was isolated from Bacillus clausii TCCC 11004, and the recombinant β-xylosidase (rXYLO) was most active at pH 8.0 and stable in a broad pH range (7.

Biochemical and Structural Properties of a High-Temperature-Active Laccase from and Its Application in the Decolorization of Food Dyes.

A novel laccase gene isolated from TCCC 11568 was expressed, and the recombinant laccase (rLAC) displayed maximal activity at 80 °C and at pH 6.0 against ABTS. rLAC maintained its structural integrity at a high temperature (355 K) compared to its tertiary structure at a low temperature (325 K), except for some minor adjustments of certain loops.