Publications by authors named "Chuanxu Guo"
Clustered surface amino acid residues modulate the acid stability of GH10 xylanase in fungi.
Appl Microbiol Biotechnol
February 2024
Article Synopsis
- Five highly acidic and thermostable GH10 xylanases were identified, with optimal temperatures between 70-90°C and stability at pH 2.0.
- Key amino acid sites responsible for acid stability were located in two main surface regions behind the enzyme's active center.
- The study provides insights into the interactions of amino acids that can improve both acid stability and thermostability in GH10 xylanases, offering targets for future genetic modifications.
Background: Filamentous fungi are highly efficient at deconstructing plant biomass by secreting a variety of enzymes, but the complex enzymatic regulation underlying this process is not conserved and remains unclear.
Results: In this study, cellulases and xylanases could specifically respond to Avicel- and xylan-induction, respectively, in lignocellulose-degrading strain Trichoderma guizhouense NJAU4742, however, the differentially regulated cellulases and xylanases were both under the absolute control of the same TgXyr1-mediated pathway. Further analysis showed that Avicel could specifically induce cellulase expression, which supported the existence of an unknown specific regulator of cellulases in strain NJAU4742.