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Bioconversion of chitin to chitosan: purification and characterization of chitin deacetylase from Mucor rouxii.
Open accessAbstract
Chitin deacetylase, the enzyme that catalyzes the hydrolysis of acetamido groups of N-acetylglucosamine in chitin, has been purified to homogeneity from mycelial extracts of the fungus Mucor rouxii and further characterized. The enzyme exhibits a low pI (approximately 3). Its apparent molecular mass was determined to be approximately 75 kDa by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and approximately 80 kDa by size-exclusion chromatography, suggesting that the enzyme exists as a monomer. Carbohydrate analysis of purified chitin deacetylase revealed that the enzyme is a high-mannose glycoprotein and that its carbohydrate content is approximately 30% by weight. Chitin deacetylase is active on several chitinous substrates and chitin derivatives. The enzyme requires at least four N-acetylglucosamine residues (chitotetraose) for catalysis, and it is inhibited by carboxylic acids, particularly acetic acid. When glycol chitin (a water-soluble chitin derivative) was used as substrate, the optimum temperature for enzyme activity was determined to be approximately 50 degrees C and the optimum pH was approximately 4.5.
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Metadata
- Authors
- Kafetzopoulos, D., Martinou, A., & Bouriotis, V
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1993-04
- Volume
- 90
- Issue
- 7
- Pages
- 2564-2568
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1995395488
- Cited by
- 254
- References
- 11
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- green
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- Kafetzopoulos, D., Martinou, A., & Bouriotis, V. (1993). Bioconversion of chitin to chitosan: purification and characterization of chitin deacetylase from Mucor rouxii. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.7.2564
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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