Enzymatic properties of β-N-acetylglucosaminidases.

Rui Zhang, Junpei Zhou, Zhifeng Song, Zunxi Huang

Journal: Applied microbiology and biotechnology 2018;102(1):93-103

PMID: 29143882

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.

Address: Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China.; College of Life Sciences, Yunnan Normal University, No. 768 Juxian Street, Chenggong, Kunming, 650500, Yunnan, People's Republic of China.; Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Kunming, 650500, Yunnan, People's Republic of China.; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China.; Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. [email protected].; College of Life Sciences, Yunnan Normal University, No. 768 Juxian Street, Chenggong, Kunming, 650500, Yunnan, People's Republic of China. [email protected].; Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Kunming, 650500, Yunnan, People's Republic of China. [email protected].; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China. [email protected].; Engineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming, 650500, People's Republic of China. [email protected].; College of Life Sciences, Yunnan Normal University, No. 768 Juxian Street, Chenggong, Kunming, 650500, Yunnan, People's Republic of China. [email protected].; Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment, Kunming, 650500, Yunnan, People's Republic of China. [email protected].; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming, 650500, People's Republic of China. [email protected].

DOI: 10.1007/s00253-017-8624-7

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

MeSH Terms: Acetylglucosamine, Acetylglucosaminidase, Amino Acid Sequence, Chitin, Chitinases, Cloning, Molecular, Enzyme Stability, Ethanol, Humans, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Phylogeny, Substrate Specificity, Tay-Sachs Disease, Temperature