Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans

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Authors
Wang, Haisheng
He, Wenqin
Jiang, Peixia
Yu, Yanlei
Lin, Lei
Sun, Xiaojun
Koffas, Mattheos
Zhang, Fuming
Linhardt, Robert J.
Issue Date
2017-10-01
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Abstract
There is a need for degradative enzymes in the study of glycosaminoglycans. Many of these enzymes are currently available either in their natural or recombinant forms. Unfortunately, progress in structure-activity studies of keratan sulfate (KS) have been impeded by the lack of a commercially available endo-β-N-acetylglucosaminidase, keratantase II. The current study uses a recently published sequence of a highly thermostable keratanase II identified in Bacillus circulans to clone and express a series of truncation mutants in Escherichia coli BL21. The resulting truncated forms of keratanase II exhibit activity and excellent storage and thermal stability making these useful tools for glycobiology research.
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Glycoconjugate Journal, 34, 643–649
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Full Citation
Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans, H. Wang, W. He, P. Jiang, Y. Yu, L. Lin, X. Sun, M. Koffas, F. Zhang, Robert J. Linhardt, Glycoconjugate Journal, 34, 643–649, 2017.
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ISSN
15734986
2820080
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