Engineering of GH11 Xylanases for Optimal pH Shifting for Industrial Applications

Endo-1,4-beta-xylanases belonging to the glycoside hydrolase (GH) 11 family hydrolyze the beta-1,4-glycosidic linkages in the xylan backbone to convert polymeric xylan into xylooligosaccharides. GH11 xylanases play an essential role in sugar metabolism and are one of the most widely used enzymes in various industries, such as pulp and paper, food and feed, biorefinery, textile, and pharmaceutical industries. pH is a crucial factor influencing the biochemical properties of GH11 xylanase and its application in bioprocessing. For the optimal pH shifting of GH11 xylanase in industrial applications, various protein engineering studies using directed evolution, rational engineering, and in silico approaches have been adopted. Here, we review the functions, structures, and engineering methods developed for the optimal pH shifting of GH11 xylanases. The various GH11 engineering techniques and key residues involved in pH shifting are discussed based on their crystal and modeled structure. This review provides an overview of recent advancements in the characterization and engineering of GH11 xylanases, providing a guide for future research in this field.

Automated summary

This review provides an overview of the importance of GH11 xylanases in bioprocessing and the key factors influencing their application. The engineering methods for achieving optimal pH shifting of GH11 xylanases in industrial applications are discussed, providing guidance for future research.