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

Authors
  • Wang, Haisheng1, 2
  • He, Wenqin2
  • Jiang, Peixia3, 4
  • Yu, Yanlei3
  • Lin, Lei3
  • Sun, Xiaojun3
  • Koffas, Mattheos2
  • Zhang, Fuming5
  • Linhardt, Robert J6, 7, 8
  • 1 Graduate School of Chinese Academy of Agricultural Sciences, People's Republic of China, Beijing, 100081, China. , (China)
  • 2 Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
  • 3 Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
  • 4 Institute of Microbiology, Chinese Academy of Sciences, Chaoyang District, Beijing, 100101, China. , (China)
  • 5 Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA. [email protected]
  • 6 Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA. [email protected]
  • 7 Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA. [email protected]
  • 8 Departments of Biology, Biomedical Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA. [email protected]
Type
Published Article
Journal
Glycoconjugate Journal
Publisher
Springer-Verlag
Publication Date
Oct 01, 2017
Volume
34
Issue
5
Pages
643–649
Identifiers
DOI: 10.1007/s10719-017-9786-3
PMID: 28752383
Source
Medline
Keywords
License
Unknown

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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