Purification and Some Properties of Metallo Proteinase from the Pilei: Essential for the Growth of Pileus and Basidiospore Formation in the Fruit Body of Flammulina velutipes
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概要
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In order to explore the relationship between proteinase and fruit body growth and basidiospore formation in mushrooms, the metallo proteinase from the pilei in the fruit bodies of Enokitake (Flammulina velutipes) was purified and characterized. The metallo proteinase was highly purified (194-fold) with a recovery of 5.90%. The enzyme was the most active at pH 6.5 toward casein, and stable only within the narrow range of pH 6.0 to 8.0 even under mild temperature (37°C, 30 min). The molecular weight and isoelectric point were found to be 18,000 and pI 6.0, respectively. The enzyme was strongly inhibited by MK-I or synthetic metallo proteinase inhibitors such as ethylenediamine-tetraacetic acid and o-phenanthroline. These characteristics were compared with those of other metallo proteinases, and the possible roles of the enzyme are discussed.
著者
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Yoshikawa Kentaro
Laboratory Of Food Microbiological Engineering Faculty Of Agriculture Kinki University
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TERASHITA Takao
Laboratory of Food Microbiological Engineering, Department of Food and Nutrition, Faculty of Agricul
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Shishiyama Jiko
Laboratory of Food Microbiology, Faculty of Agriculture, Kinki University
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TERASHITA Takao
Laboratory of Food Microbiology, Faculty of Agriculture, Kinki University
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