ArticleBMC biotechnology2017
Distinctive molecular and biochemical characteristics of a glycoside hydrolase family 20 β-N-acetylglucosaminidase and salt tolerance.
Article in BMC biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 21 citations in OpenAlex.
- Characterization of a New Multifunctional GH20 β-Frontiers in microbiology · 2022Article
- High-Level Extracellular Expression of a New β-N-Acetylglucosaminidase inFrontiers in microbiology · 2021Article
- Identification and Characterization of a β-International journal of molecular sciences · 2020Article
- Examining the molecular characteristics of glycoside hydrolase family 20 β-N-acetylglucosaminidases with high activity.Bioengineered · 2019Article
- Zinc binding proteome of a phytopathogenRoyal Society open science · 2019Article
- Combined Detection of Urinary Micro Albumin, α1-microglobulin and N-acetyl-β-D-glucosaminidase in the Early Diagnosis of Diabetic Nephropathy.Pakistan journal of medical sciencesArticle
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundEnzymatic degradation of chitin has attracted substantial attention because chitin is an abundant renewable natural resource, second only to lignocellulose, and because of the promising applications of N-acetylglucosamine in the bioethanol, food and pharmaceutical industries. However, the low activity and poor tolerance to salts and N-acetylglucosamine of most reported β-N-acetylglucosaminidases limit their applications. Mining for novel enzymes from new microorganisms is one way to address this problem.
resultsA glycoside hydrolase family 20 (GH 20) β-N-acetylglucosaminidase (GlcNAcase) was identified from Microbacterium sp. HJ5 harboured in the saline soil of an abandoned salt mine and was expressed in Escherichia coli. The purified recombinant enzyme showed specific activities of 1773.1 ± 1.1 and 481.4 ± 2.3 μmol min
conclusionsBiochemical characterization revealed that the GlcNAcase had novel salt-GlcNAc tolerance and high activity. These characteristics suggest that the enzyme has versatile potential in biotechnological applications, such as bioconversion of chitin waste and the processing of marine materials and saline foods. Molecular characterization provided an understanding of the molecular-function relationships for the salt tolerance and high activity of the GH 20 GlcNAcase.
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