Glycosylation of cellulase: a novel strategy for improving cellulase

Protein glycosylation is the most complex posttranslational modification process. Most cellulases from filamentous fungi contain N-glycosylation and O-glycosylation. Here, we discuss the potential roles of glycosylation on the characteristics and function of cellulases. The use of certain cultivation, inducer, and alteration of engineering glycosylation pathway can enable the rational control of cellulase glycosylation. Glycosylation does not occur arbitrarily and may tend to modify the 3D structure of cellulases by using specially distributed glycans. Therefore, glycoengineering should be considered comprehensively along with the spatial structure of cellulases. Cellulase glycosylation may be an evolution phenomenon, which has been considered as an economical way for providing different functions from identical proteins. In addition to gene and transcription regulations, glycosylation may be another regulation on the protein expression level. Enhanced understanding of the potential regulatory role of cellulase glycosylation will enable synthetic biology approaches for the development of commercial cellulase.

Automated summary

Protein glycosylation is a complex posttranslational modification process. Cellulases from fungi contain N-glycosylation and O-glycosylation. This study discusses the potential roles of glycosylation on cellulase characteristics and function. Glycoengineering can be used to control cellulase glycosylation by modifying the 3D structure through specially distributed glycans. Understanding the regulatory role of cellulase glycosylation will enable synthetic biology approaches for commercial cellulase development.