Glycosylation of cellulase: a novel strategy for improving cellulase

Abstract

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.

Keywords:

• Cellulase
• posttranslational modification
• glycosylation
• N-glycosylation
• O-glycosylation
• glycoengineering

Disclosure statement

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Additional information

Funding

This work was supported by National Key R&D Program of China [No. 2018YFA0900500], Jilin Province and Chinese Academy of Sciences Science and Technology Cooperation High-tech Industrialization Fund Project [2022SYHZ0015 and 2022SYHZ0019], and Liaoning Province Natural Science Foundation [2020-MS-276].