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Enzymatic properties of β-N-acetylglucosaminidases

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Abstract

β-N-Acetylglucosaminidases (GlcNAcases) hydrolyse N-acetylglucosamine-containing oligosaccharides and proteins. These enzymes produce N-acetylglucosamine (GlcNAc) and have a wide range of promising applications in the food, energy, and pharmaceutical industries, such as synergistic degradation of chitin with endo-chitinases and using GlcNAc to produce sialic acid, bioethanol, single-cell proteins, and pharmaceutical therapeutics. GlcNAcases also play an important role in the dynamic balance of cellular O-linked GlcNAc levels, catabolism of ganglioside storage in Tay–Sachs disease, and bacterial cell wall recycling and flagellar assembly. In view of these important biological functions and the wide range of industrial applications of GlcNAcases, this review aims to provide a better understanding of various advances for these enzymes. It focuses on enzymatic properties of GlcNAcases, including substrate specificity, catalytic activity, pH optimum, temperature optimum, thermostability, the effects of various metal ions and organic reagents, and transglycosylation.

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Funding

This work was supported by the National Key Research and Development Program of China (grant no. 2017YFB0308401), the Yunling Scholars (grant no. 2015 56), the Yunling Industry Leading Talents (grant no. 2014 1782), the Reserve Talents Project for Young and Middle-Aged Academic and Technical Leaders of Yunnan Province (grant no. 2015HB033), and the Applied and Basic Research Foundation of Yunnan Province (grant no. 201401PC00224).

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Correspondence to Junpei Zhou or Zunxi Huang.

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The authors declare that they have no competing interests.

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This article does not contain any studies with human participants or animals performed by any of the authors.

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Zhang, R., Zhou, J., Song, Z. et al. Enzymatic properties of β-N-acetylglucosaminidases. Appl Microbiol Biotechnol 102, 93–103 (2018). https://doi.org/10.1007/s00253-017-8624-7

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  • DOI: https://doi.org/10.1007/s00253-017-8624-7

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