PURIFICATION AND CHARACTERISTICS OF MEMBRANE-BOUND CHITINASE OF ANAEROBIC RUMINAL FUNGUS PIROMYCES-COMMUNIS OTS1

Citation
M. Sakurada et al., PURIFICATION AND CHARACTERISTICS OF MEMBRANE-BOUND CHITINASE OF ANAEROBIC RUMINAL FUNGUS PIROMYCES-COMMUNIS OTS1, Current microbiology, 37(1), 1998, pp. 60-63
Citations number
18
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
ISSN journal
0343-8651
Volume
37
Issue
1
Year of publication
1998
Pages
60 - 63
Database
ISI
SICI code
0343-8651(1998)37:1<60:PACOMC>2.0.ZU;2-I
Abstract
A membrane-bound chitinase from cell wall fractions of the anaerobic r uminal fungus, Piromyces communis OTS1, was purified by affinity chrom atography, gel filtration, and chromatofocusing. The molecular size of the chitinase was estimated by gel filtration to be 42.4 kDa and by S DS-PAGE to be 44.8 kDa, and its pI was 4.4. Activity was inhibited by Hg2+ and allosamidin. The activity at 39 degrees C was greatest at pH 6.0. It had an 'endo' type action. Solubilization tests indicated that plasmalemma-bound chitinase was held in place by an electrostatic typ e interaction. Characterization of the membrane-bound chitinase was mo re similar to that of extracellular chitinase than cytosolic chitinase . This suggested that membrane-bound chitinase was the origin of extra cellular chitinase.