title: Endochitinase from Aspergillus nidulans implicated in the autolysis of its cell wall.
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.
authors.affiliation: Unidad de Microbiologia Aplicada, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
authors.forename: F
authors.initials: F
authors.lastname: Reyes
authors.forename: J
authors.initials: J
authors.lastname: Calatayud
authors.forename: M J
authors.initials: MJ
authors.lastname: Martinez
mesh_terms: D001233:Aspergillus nidulans / Q000201:enzymology*; D002473:Cell Wall / Q000378:metabolism; D002686:Chitin / Q000378:metabolism; D002688:Chitinases / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid
chemical_list: D002686:Chitin; D002688:Chitinases