A putative protease gene (aprE) from the thermophilic bacterium Coprothermobacter proteolyticus was cloned and expressed in Bacillus subtilis. The enzyme was determined to be a serine protease based on inhibition by PMSF. Biochemical characterization demonstrated that the enzyme had optimal activity under alkaline conditions (pH 8-10). In addition, the enzyme had an elevated optimum temperature...

Proteases are important industrial enzymes used in different areas of industry, mainly detergent, food and leather industries. In this study, novel alkaline protease-producing bacterium was isolated from Geinarje hot spring and examined for maximum protease activity to be utilized in washing-powder. The isolated bacterium was cultured in mineral salt medium including 2% Skim Milk. Proteolytic a...

The genome sequence of alkalohalophilic actinobacterium Nocardiopsis sinuspersici UTMC102 is provided. N. sinuspersici UTMC102 produces a highly active serine alkaline protease, and contains at least 11 gene clusters encoding the biosynthesis of secondary metabolites. The N. sinuspersici UTMC102 genome was assembled into a single chromosomal scaffold.

Proteolytic enzymes have evolved several mechanisms to cleave peptide bonds. These distinct types have been systematically categorized in the MEROPS database. While a BLAST search on these proteases identifies homologous proteins, sequence alignment methods often fail to identify relationships arising from convergent evolution, exon shuffling, and modular reuse of catalytic units. We have previ...

A number of isolates of Aspergillus fumigatus obtained from the hospital environment produced extracellular elastolytic activity. This activity was found to be catalyzed by a single 33-kDa protein which was purified and characterized to be a serine protease. A. fumigatus, when grown on the insoluble structural material obtained from murine and bovine lung, produced the same extracellular 33-kDa...

Alkaline protease from a mutant of Bacillus licheniformis Bl8 was purified from the culture supernatant by employing the methods such as ammonium sulphate precipitation, DEAE cellulose chromatography followed by Gel filtration using Sephadex G-100. The yield of the enzyme after purification was found to be 10%. Protease was found to be homogenous when examined by SDS-PAGE and the enzyme showed ...

Plg (plasminogen), a member of the serine protease superfamily, is a key component constituting the fibrinolytic system, and its evolutionary origin remains unknown during the course of animal evolution. In the present study, we isolated a cDNA, designated BbPlgl, encoding a kringle-containing protease with plasminogen-like activity from the basal chordate Branchiostoma belcheri. The deduced pr...