Some Properties of Endo-polygalacturonase from Trichosporon penicillatum SNO-3
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概要
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Some properties of the endo-polygalacturonase from Trichosporon penicillatum were investigated. The enzyme showed the highest activity around pH 5.0 and was stable at this pH up to 50°C. The enzyme catalyzed the hydrolysis of galacturonic acid oligomers as well as its polymer. The pentamer was degraded to a trimer and a dimer, the tetramer to a trimer and a monomer, and the trimer to a dimer and a monomer, respectively, whereas the dimer was not degraded. The kinetic constant Vmax and Km values changed with the substrate chain-length; the Km values tended to decrease, whereas the Vmax values tended to increase with increasing chain-length of the substrate. The amino acid residue participating in the active site of the enzyme was studied and it was found to be histidine.
- 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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SAWADA Masahiko
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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OKUSHIMA Minoru
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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