N‐glycosylation affects the proper folding, enzymatic characteristics and production of a fungal β‐glucosidase. Issue 12 (1st August 2013)

• Record Type: Journal Article
• Authors: Wei, Wei; Chen, Ling; Zou, Gen; Wang, Qianfu; Yan, Xing; Zhang, Jun; Wang, Chengshu; Zhou, Zhihua
• Is Part Of: Biotechnology and bioengineering. Volume 110:Issue 12(2013:Dec.)
• Page Start: 3075
• Page End: 3084
• Publication Date: 2013-08-01
• Subjects: Biotechnology -- Periodicals; Bioengineering -- Periodicals; 660.6
• DOI: 10.1002/bit.24990
• Languages: English
• ISSNs: 0006-3592

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>ABSTRACT</title> <sec id="bit24990-sec-0001" sec-type="section"> <p>Heterologous expression of β‐glucosidase is one of the approaches to enhance the efficiency of fungal cellulase preparations. It has been reported that <italic>N</italic>‐glycosylation affects the structure framework, function and stability of proteins. In this study, a β‐glucosidase from <italic>Aspergillus terreus</italic> (GenBank: XP_001216552, BglS) was heterologously expressed in <italic>Pichia pastoris</italic> and <italic>Trichoderma reesei</italic>. The four asparagine residues were all linked with high‐mannose‐type oligosaccharides in <italic>P. pastoris</italic>, whereas only N224 carried high‐mannose‐type glycan in <italic>T. reesei</italic> (the other three sites carried one <italic>N</italic>‐acetylglucosamine). The long <italic>N</italic>‐glycan chains on PpBglS weakened its substrate affinity, activity and thermostability. The moderate post‐translational and post‐secretory glycan modification in <italic>T. reesei</italic> 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 <italic>N</italic>‐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.</p> </sec> </abstract>