PROTEINASES FROM THE FRUIT-BODY OF FLAMMU LINA VELUTIPES

In order to clarify the relationships between the proteinase and the f ruit-body growth and basidiospore formation in mushroom, we studied th e proteinase in the fruit-body of Flammulina velutipes cultured in pot ato dextrose liquid medium, and following results were obtained. (1) A cid and neutral proteinase with optimum pHs of 3.2 and 6.5 was found i n the fruit-body. Both the enzymes exhibited increased dramatically ac tivities in the pileus (12 times) but did not show significant activit ies change in stipe during the fruit-body growth. When comparing the a ctivities of both the enzymes, the total activity and specific activit y of neutral proteinase was 4 times and 3.3 times greater than that of acid proteinase enzyme, respectively. (2) When treated with various t ypes of proteinase inhibitors for elucidation the type of enzyme, it w as observed that acid proteinase to be carboxyl type and neutral prote inase having metal type. The isoelectric point of the metal type enzym e was pH 6.0. From the above observations, it was concluded that the m etal proteinase having pi 6.0 was important for the fruit-body growth and also exhibits significant role in basidiospore formation.