Shimogaki H, Takeuchi K, Nishino T, Ohdera M, Kudo T, Ohba K, Iwama M, Irie M
Biological Science Laboratories, Lion Corporation, Kanagawa, Japan.
Agric Biol Chem. 1991 Sep;55(9):2251-8.
In the course of a search for an alkaline stable protease for industrial use, an alkaline protease (protease BYA) was isolated from an alkalophilic Bacillus sp. Y, and its properties were characterized. Its optimum pH was pH 10.0-12.5, when casein was used as a substrate. In addition to the stability of protease BYA at pH 6.5-13.0, it was also very stable towards various surface-active agents, such as sodium dodecyl sulfate and sodium linear alkylbenzene sulfonate. Protease BYA was most active at 70 degrees C. The isoelectric point (pI) of protease BYA was about 10.1. Protease BYA was characterized as a serine protease because of its sensitivity to phenylmethanesulfonyl fluoride and diisopropyl fluorophosphate. The protease seems to be related to proteases of the subtilisin family, such as subtilisin BPN', subtilisin Carlsberg, and No. 221 protease.
在寻找一种用于工业用途的碱性稳定蛋白酶的过程中，从嗜碱芽孢杆菌Y中分离出一种碱性蛋白酶（蛋白酶BYA），并对其性质进行了表征。当以酪蛋白为底物时，其最适pH为10.0 - 12.5。除了蛋白酶BYA在pH 6.5 - 13.0下的稳定性外，它对各种表面活性剂，如十二烷基硫酸钠和直链烷基苯磺酸钠也非常稳定。蛋白酶BYA在70℃时活性最高。蛋白酶BYA的等电点（pI）约为10.1。蛋白酶BYA由于对苯甲磺酰氟和二异丙基氟磷酸敏感，被表征为丝氨酸蛋白酶。该蛋白酶似乎与枯草杆菌蛋白酶家族的蛋白酶有关，如枯草杆菌蛋白酶BPN'、枯草杆菌蛋白酶卡尔伯格和221号蛋白酶。
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