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

Authors
Wang, Haisheng
He, Wenqin
Jiang, Peixia
Yu, Yanlei
Lin, Lei
Sun, Xiaojun
Koffas, Mattheos
Zhang, Fuming
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2017-10-01
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
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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.
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.
Description
Glycoconjugate Journal, 34, 643–649
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Glycoconjugate Journal
https://harc.rpi.edu/
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