title: Purification and characteristics of an autolytic chitinase of Piromyces communis OTS1 from culture medium.
abstract: An autolysis chitinase was purified from the cultural medium of the anaerobic fungus Piromyces communis OTS1 by ammonium sulfate precipitation, affinity chromatography with regenerated chitin, chromato-focusing, gel filtration, and chromato-focusing again. The optimal pH and temperature were 6.0 and 50 degrees C, respectively, for a 20-min assay. The chitinase was stable from pH 6.0 to 8.0, but was unstable at 70 degrees C for 20 min. The molecular mass of chitinase was estimated by SDS-PAGE to be 44.9 kDa, and its pI was 4.4. The enzyme activity, which was of the 'endo' type, was inhibited by Hg2+ and allosamidin. The chitinase hydrolyzes chitin powder and fungal cell walls at a higher rate than an artificial chitin substrate. It can be concluded that extracellular chitinase is similar to cytosolic chitinase, but they are not the same protein.
authors.affiliation: Laboratory of Animal Nutrition and Biochemistry, Animal Science Division, Faculty of Agriculture, Miyazaki University, Nishi 1-1, Gakuen Kibana-dai, Miyazaki 889-21, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Sakurada
authors.forename: D P
authors.initials: DP
authors.lastname: Morgavi
authors.forename: K
authors.initials: K
authors.lastname: Komatani
authors.forename: Y
authors.initials: Y
authors.lastname: Tomita
authors.forename: R
authors.initials: R
authors.lastname: Onodera
mesh_terms: D002688:Chitinases / Q000302:isolation & purification*; D003470:Culture Media; D005658:Fungi / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity
chemical_list: D003470:Culture Media; D002688:Chitinases