Biomaterial Database

Extracellular serine protease synthesis by mosquito-pathogenic strains of Bacillus sphaericus. 1993

C Dumusois, and F G Priest

Department of Biological Sciences, Heriot-Watt University, Edinburgh, UK.

Nine strains of Bacillus sphaericus toxic to mosquito larvae produced haloes of hydrolysis when cultured on casein-nutrient agar. In batch culture, protease synthesis by B. sphaericus BSE 18 occurred during exponential growth and was repressed by high concentrations of peptone. Extracellular protease from this bacterium showed optimal activity at about pH 10.2, was inhibited by phenylmethylsulphonyl chloride and chymostatin but not soybean trypsin inhibitor or EDTA. Hydrolysis of N-CBZ-glycine-nitrophenyl ester was consistent with the major enzyme being a serine protease.

UI	MeSH Term	Description	Entries
D009033	Culicidae	A family of the order DIPTERA that comprises the mosquitoes. The larval stages are aquatic, and the adults can be recognized by the characteristic WINGS, ANIMAL venation, the scales along the wing veins, and the long proboscis. Many species are of particular medical importance.	Mosquitoes,Mosquitos,Mosquito
D010572	Pest Control, Biological	Use of naturally-occuring or genetically-engineered organisms to reduce or eliminate populations of pests.	Biological Pest Control,Biologic Pest Control,Pest Control, Biologic,Biologic Pest Controls,Biological Pest Controls,Pest Controls, Biologic,Pest Controls, Biological
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001407	Bacillus	A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic.	Bacillus bacterium
D012697	Serine Endopeptidases	Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.	Serine Endopeptidase,Endopeptidase, Serine,Endopeptidases, Serine