Purification and Characteristics of Membrane-Bound Chitinase of Anaerobic Ruminal Fungus Piromyces communis OTS1 |
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Authors: | Masaru Sakurada Diego P Morgavi Naomi Ushirone Kenji Komatani Yoshifumi Tomita Ryoji Onodera |
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Institution: | (1) Laboratory of Animal Nutrition and Biochemistry, Faculty of Agriculture, Miyazaki University, Miyazaki 889-21, Japan , JP;(2) Rowett Research Institute, Bucksburn, Aberdeen, AB2 9SB, Scotland, UK , UK |
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Abstract: | A membrane-bound chitinase from cell wall fractions of the anaerobic ruminal fungus, Piromyces communis OTS1, was purified by affinity chromatography, gel filtration, and chromatofocusing. The molecular size of the chitinase
was estimated by gel filtration to be 42.4 kDa and by SDS-PAGE to be 44.8 kDa, and its pI was 4.4. Activity was inhibited
by Hg2+ and allosamidin. The activity at 39°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 type interaction. Characterization of the membrane-bound
chitinase was more similar to that of extracellular chitinase than cytosolic chitinase. This suggested that membrane-bound
chitinase was the origin of extracellular chitinase.
Received: 15 October 1997 / Accepted: 13 January 1998 |
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