Open AccessCharacterization of pyrolysin, a hyperthermoactive serine protease from the archaebacterium Pyrococcus furiosus
Author(s) -
Eggen Rik,
Geerling Ans,
Watts Jennifer,
Vos Willem M.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb03791.x
Subject(s) - pyrococcus furiosus , serine protease , protease , biochemistry , masp1 , thermophile , chemistry , serine , biology , enzyme , archaea , gene
From the hyperthermophilic archaebacterium Pyrococcus furiosus an oxygen‐stable, extremely thermostable protease activity, which we designate pyrolysin, has been identified and characterized. Pyrolysin is a cell‐envelope associated protease activity high thermo‐activity and stability. The temperature optimum is 115°C and half‐life values in the absence of substrate are: at least 96 h at 80°C, 9 h at 95°C, 4h at 100°C, 20 min at 105°C and 3 min at 110°C. Pyrolysin is active at a broad pH range between 6.5 and 10.5, and was classified as a serine‐type protease activity. Zymogram staining showed the presence of multiple protease bands of about 140, 130, 115, 100 and 65 kDa.