Endochitinase from Aspergillus nidulans implicated in the autolysis of its cell wall |
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Authors: | Fuensanta Reyes Jose Calatayud Maria Jesus Martinez |
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Institution: | Unidad de Microbiologia Aplicada, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain. |
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Abstract: | An endochitinase from centrifuged autolyzed cultures of Aspergillus nidulans has been purified 100 times. The enzyme has Mw 27,000, pI of 4.8 units, pH optimum around 5 pH units. It is unstable at temperature greater than 70 degrees C and does not have a cation requirement. It is inhibited by Hg2+, Cu2+, Ca2+ and Ag+ and it does not have muramidase activity. The enzyme depolymerizes chitin rapidly with production of high molecular weight polysaccharides, and then slowly degrades these with production of N,N'-diacetylchitobiose. The enzyme hydrolyzes N,N',N'-triacetylchitotriose with production of N,N'-diacetylchitobiose and N-acetylglucosamine and this hydrolysis is inhibited by other chitin oligomers and N-acetylglucosamine. This enzyme hydrolyzes in the same way the chitin obtained from the cell wall of Aspergillus nidulans. |
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Keywords: | Endochitinase Aspergillus nidulans Autolysis |
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