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.
journal_name
Curr Microbioljournal_title
Current microbiologyauthors
Sakurada M,Morgavi DP,Komatani K,Tomita Y,Onodera Rdoi
10.1007/s002849900210subject
Has Abstractpub_date
1997-07-01 00:00:00pages
48-51issue
1eissn
0343-8651issn
1432-0991journal_volume
35pub_type
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