Purification and characteristics of cytosolic chitinase from Piromyces communis OTS1.
A chitinase was purified from the cytosolic fraction of the anaerobic rumen fungus Piromyces communis OTS1 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 'endo' type, was inhibited by Ag+, Hg2+ and allosamidin. N-Acetyl-beta-glucosaminidase and 'exo' type chitinase activity were absent from the purified preparation.
Sakurada
M
M
Faculty of Agriculture, Miyazaki University, Japan.
Morgavi
D P
DP
Komatani
K
K
Tomita
Y
Y
Onodera
R
R
D000818:Animals; D002688:Chitinases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D003600:Cytosol / Q000201:enzymology; D005658:Fungi / Q000201:enzymology* / Q000302:isolation & purification; D006041:Goats; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D012417:Rumen / Q000382:microbiology; D013379:Substrate Specificity
D002688:Chitinases