Purification and SomeProperties of a Protopectin-solubilizing Enzymefrom Galactomyces reessii Strain L
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概要
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Galactomyces reessii L, isolated as a protopectin-solubilizing enzyme-producing strain, produced protopectin-solubilizing enzyme in the culture filtrate. The enzyme was purified by repeated CM-Sephadex C-50 column chromatography, and isolated as a crystalline form with a yield of 16% of the initial activity. The enzyme was a glycoprotein containing about 2.6% carbohydrate (as pentose). Its isoelectric point was around pH 8.4, and the sedimentation coefficient (s20, w) was determined to be 3.83 S. The molecular weight was determined to be 30, 000 by gel filtration on Sephadex G-75 and 29, 300 by ultracentrifugal analysis. The enzyme catalyzed the release of highly polymerized pectin from various protopectins. The enzyme also catalyzed the depolymerization of pectic acid or galacturonic acid oligomers, and was confirmed to be an endopolygalacturonase.
- 社団法人 日本農芸化学会の論文
著者
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Sakai Takuo
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Yoshitake Shinobu
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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