PURIFICATION AND CHARACTERISTICS OF AN AUTOLYTIC CHITINASE OF PIROMYCES-COMMUNIS-OTS1 FROM CULTURE-MEDIUM

Citation
M. Sakurada et al., PURIFICATION AND CHARACTERISTICS OF AN AUTOLYTIC CHITINASE OF PIROMYCES-COMMUNIS-OTS1 FROM CULTURE-MEDIUM, Current microbiology, 35(1), 1997, pp. 48-51
Citations number
24
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
ISSN journal
0343-8651
Volume
35
Issue
1
Year of publication
1997
Pages
48 - 51
Database
ISI
SICI code
0343-8651(1997)35:1<48:PACOAA>2.0.ZU;2-4
Abstract
An autolysis chitinase was purified from the cultural medium of the an aerobic fungus Piromyces communis OTS I by ammonium sulfate precipitat ion, affinity chromatography with regenerated chitin, chromate-focusin g, gel filtration, and chromato-focusing again. The optimal pH and tem perature 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 de grees C for 20 min, The molecular mass of chitinase was estimated by S DS-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 ch itinase hydrolyzes chitin powder and fungal cell walls at a higher rat e than an artificial chitin substrate. It can be concluded that extrac ellular chitinase is similar to cytosolic chitinase, but they are not the same protein.