This article was published online on 1 August 2013. Subsequently, an error was found and the correction was published on 16 August 2013.
N-glycosylation affects the proper folding, enzymatic characteristics and production of a fungal β-glucosidase
Article first published online: 1 AUG 2013
© 2013 Wiley Periodicals, Inc.
Biotechnology and Bioengineering
Volume 110, Issue 12, pages 3075–3084, December 2013
How to Cite
Wei, W., Chen, L., Zou, G., Wang, Q., Yan, X., Zhang, J., Wang, C. and Zhou, Z. (2013), N-glycosylation affects the proper folding, enzymatic characteristics and production of a fungal β-glucosidase. Biotechnol. Bioeng., 110: 3075–3084. doi: 10.1002/bit.24990
Wei Wei and Ling Chen contributed equally to this work.
- Issue published online: 23 OCT 2013
- Article first published online: 1 AUG 2013
- Accepted manuscript online: 8 JUL 2013 06:32AM EST
- Manuscript Accepted: 24 JUN 2013
- Manuscript Revised: 17 JUN 2013
- Manuscript Received: 10 MAY 2013
- National Basic Research Program of China (973 program):. Grant Numbers: 2011CB707403, 2012CB721103
- Knowledge Innovation Program. Grant Numbers: KSCX2-EW-G-13-1, KSCX2-EW-J-12
- International Joint Research Program. Grant Number: GJHZ1128
- Pichia pastoris;
- Trichoderma reesei;
- enzymatic characteristics;
- native folding
Heterologous expression of β-glucosidase is one of the approaches to enhance the efficiency of fungal cellulase preparations. It has been reported that N-glycosylation affects the structure framework, function and stability of proteins. In this study, a β-glucosidase from Aspergillus terreus (GenBank: XP_001216552, BglS) was heterologously expressed in Pichia pastoris and Trichoderma reesei. The four asparagine residues were all linked with high-mannose-type oligosaccharides in P. pastoris, whereas only N224 carried high-mannose-type glycan in T. reesei (the other three sites carried one N-acetylglucosamine). The long N-glycan chains on PpBglS weakened its substrate affinity, activity and thermostability. The moderate post-translational and post-secretory glycan modification in T. reesei makes it a suitable expression system for BglS. The N224 glycan played a critical role in BglS folding. The elucidation of the correlation between the different N-glycosylation patterns of BglS and their corresponding enzymatic characteristics is an important step towards improving the activity, thermostability and even production of heterologous β-glucosidase by glycan engineering. Biotechnol. Bioeng. 2013;110: 3075–3084. © 2013 Wiley Periodicals, Inc.