Purification and Characterization of Alkaline Serine Proteinase from Photosynthetic Bacterium, Rubrivivax gelatinosus KDDS1
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概要
- 論文の詳細を見る
In order to reduce the protein content of wastewater, photosynthetic bacteria producing proteinases were screened from wastewater of various sources and stocked in culture. An isolated strain, KDDS1, was identified as Rubrivivax gelatinosus, a purple nonsulfur bacterium that secretes proteinase under micro-aerobic conditions under light at 35°C. Molecular weight of the purified enzyme was estimated to be 32.5 kDa. The enzyme showed the highest activity at 45°C and pH 9.6, and the activity was completely inhibited by phenylmethyl sulfonyl fluoride (PMSF), but not by EDTA. The amino-terminal 24 amino acid sequence of the enzyme showed about 50% identity to those of serine proteinases from Pseudoalteromonas piscicida strain O-7 and Burkholderia pseudomallei. Thus, the enzyme from Rvi. gelatinosus KDDS1 was thought to be a serine-type proteinase. This was the first serine proteinase characterized from photosynthetic bacteria.
- 社団法人 日本農芸化学会の論文
- 2004-03-23
著者
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ODA Kohei
Department of Applied Biology, Kyoto Institute of Technology
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NOPARATNARAPORN NAPAVARN
Department of Microbiology, Kasetsart University
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Tanskul Somporn
Department Of Applied Biology Kyoto Institute Of Technology
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Oyama Hiroshi
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Noparatnaraporn Napavarn
Department Of Microbiology Kasetsart University
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Noparatnaraporn Napavarn
Department Of Microbiology Faculty Of Science Kasetsart University
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Oda Kohei
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Oda Kohei
Department Of Applied Biology Kyoto Institute Of Technology
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Oyama Hiroshi
Department Of Applied Biology Kyoto Institute Of Technology
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