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

    Author
    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
    Date Issued
    2017-10-01
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    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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    URI
    https://doi.org/10.1007/s10719-017-9786-3; https://hdl.handle.net/20.500.13015/5614
    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; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Glycoconjugate Journal; https://harc.rpi.edu/;
    Access
    https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s10719-017-9786-3;
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