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Expression, Purification, and Characterization of Endo-β-N-Acetylglucosaminidase H Using Baculovirus-Mediated Silkworm Protein Expression System
Bibliographic Information
- Published
- 2014-03-06
- Rights Information
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- http://www.springer.com/tdm
- DOI
-
- 10.1007/s12010-014-0814-5
- Publisher
- Springer Science and Business Media LLC
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Description
Endo-β-N-acetylglucosaminidase (Endo H) from Streptomyces plicatus hydrolyzes the core di-GlcNAc units of asparagine-linked oligosaccharides and is regarded as an important tool for glycobiology research. In the present study, we established a large-scale system to produce secreted Endo H using a silkworm-baculovirus expression system (silkworm-BES). The recombinant Endo H purified from silkworm hemolymph had activity comparable to that from recombinant Escherichia coli. As well as its well-characterized substrate RNase B, the Endo H from silkworm-BES was able to deglycosylate the high-mannose glycoproteins from silkworm hemolymph. Interestingly, the secretion amount of recombinant Endo H was significantly varied among the different silkworm strains, which could provide valuable information for larger-scale protein productions from silkworm-BES.
Journal
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- Applied Biochemistry and Biotechnology
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Applied Biochemistry and Biotechnology 172 (8), 3978-3988, 2014-03-06
Springer Science and Business Media LLC
