β-N-Acetylglucosaminidase MthNAG from Myceliophthora thermophila C1, a thermostable enzyme for production of N-acetylglucosamine from chitin
| Autor: | Martijn J. Koetsier, Gerrit Eggink, Carmen G. Boeriu, Lambertus A.M. van den Broek, Malgorzata Krolicka, Sandra W.A. Hinz |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Bio Process Engineering Sordariales Chitin Applied Microbiology and Biotechnology Acetylglucosamine Substrate Specificity N-Acetylglucosamine Chitosan Industrial Microbiology 03 medical and health sciences chemistry.chemical_compound BBP Sustainable Chemistry & Technology Acetylglucosaminidase Biobased Products Biotechnologically Relevant Enzymes and Proteins Thermostability VLAG chemistry.chemical_classification biology Chitinases Substrate (chemistry) General Medicine Hydrogen-Ion Concentration biology.organism_classification carbohydrates (lipids) 030104 developmental biology Enzyme BBP Bioconversion chemistry Biochemistry Chitinase biology.protein BBP Biorefinery & Sustainable Value Chains β-N-Acetylglucosaminidase Myceliophthora thermophila C1 Biotechnology Myceliophthora thermophila |
| Zdroj: | Applied Microbiology and Biotechnology 102 (2018) 17 Applied Microbiology and Biotechnology, 102(17), 7441-7454 Applied Microbiology and Biotechnology |
| ISSN: | 0175-7598 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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