Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 538986
Title β-N-Acetylglucosaminidase MthNAG from Myceliophthora thermophila C1, a thermostable enzyme for production of N-acetylglucosamine from chitin
Author(s) Krolicka, Malgorzata; Hinz, Sandra W.A.; Koetsier, Martijn J.; Eggink, Gerrit; Broek, Lambertus A.M. van den; Boeriu, Carmen G.
Source Applied Microbiology and Biotechnology 102 (2018)17. - ISSN 0175-7598 - p. 7441 - 7454.
DOI https://doi.org/10.1007/s00253-018-9166-3
Department(s) Bioprocess Engineering
Biobased Products
FBR Bioconversion
FBR BP Biorefinery & Sustainable Value Chains
VLAG
FBR Sustainable Chemistry & Technology
Publication type Refereed Article in a scientific journal
Publication year 2018
Keyword(s) Chitin - Chitosan - Myceliophthora thermophila C1 - N-Acetylglucosamine - β-N-Acetylglucosaminidase
Abstract

Thermostable enzymes are a promising alternative for chemical catalysts currently used for the production of N-acetylglucosamine (GlcNAc) from chitin. In this study, a novel thermostable β-N-acetylglucosaminidase MthNAG was cloned and purified from the thermophilic fungus Myceliophthora thermophila C1. MthNAG is a protein with a molecular weight of 71 kDa as determined with MALDI-TOF-MS. MthNAG has the highest activity at 50 °C and pH 4.5. The enzyme shows high thermostability above the optimum temperature: at 55 °C (144 h, 75% activity), 60 °C (48 h, 85% activity; half-life 82 h), and 70 °C (24 h, 33% activity; half-life 18 h). MthNAG releases GlcNAc from chitin oligosaccharides (GlcNAc)2–5, p-nitrophenol derivatives of chitin oligosaccharides (GlcNAc)1–3-pNP, and the polymeric substrates swollen chitin and soluble chitosan. The highest activity was detected towards (GlcNAc)2. MthNAG released GlcNAc from the non-reducing end of the substrate. We found that MthNAG and Chitinase Chi1 from M. thermophila C1 synergistically degraded swollen chitin and released GlcNAc in concentration of approximately 130 times higher than when only MthNAG was used. Therefore, chitinase Chi1 and MthNAG have great potential in the industrial production of GlcNAc.

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