PURIFICATION AND CHARACTERISTICS OF CYTOSOLIC CHITINASE FROM PIROMYCES-COMMUNIS OTS1

Citation
M. Sakurada et al., PURIFICATION AND CHARACTERISTICS OF CYTOSOLIC CHITINASE FROM PIROMYCES-COMMUNIS OTS1, FEMS microbiology letters, 137(1), 1996, pp. 75-78
Citations number
14
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
ISSN journal
0378-1097
Volume
137
Issue
1
Year of publication
1996
Pages
75 - 78
Database
ISI
SICI code
0378-1097(1996)137:1<75:PACOCC>2.0.ZU;2-J
Abstract
A chitinase was purified from the cytosolic fraction of the anaerobic rumen fungus Piromyces communis OTSl by affinity chromatography using regenerated chitin, gel filtration and chromatofocusing. The chitinase was most active at pH 6.2 and at 60 degrees C in a 20-min assay. The molecular mass of the purified protein was estimated by SDS-PAGE to be 42 kDa and its pi was 4.9. The enzyme activity, which was of the 'end o' type, was inhibited by Ag+, Hg2+ and allosamidin. N-Acetyl-beta-glu cosaminidase and 'exo' type chitinase activity were absent from the pu rified preparation.