A gene encoding an alkaline protease was cloned from an alkalophilic bacillus, and its nucleotide sequence was determined. The cloned gene was used to increase the copy number of the protease gene on the chromosome by an improved gene amplification technique.

PURPOSE To determine the effects of exoproducts from the corneal pathogen Pseudomonas aeruginosa on corneal proteinases and proteins. METHODS Whole rabbit corneas were cultured in the presence or absence of broths conditioned with Pseudomonas aeruginosa, elastase, alkaline protease, and exotoxin A. Protein synthesis was assayed by adding 35S-methionine during the last 6 hours of culture. Case...

This study was conduction to find a suitable and cheap plant as a source for extracting vegetable protease enzymes and investigate the effect of these enzymes for producing whey protein hydrolysate. The extract prepared from the composite weed cichorium pumilum had a satisfactory protease activity, each ml of this extract prepared from 0.1 gm dried cichorium weed stems.An alkaline and acidic ci...

An alkaline protease producing bacterial strain Bacillus licheniformis (MTCC NO. 7053), which was obtained from IMTECH, Chandigarh used for protease production studies. Three significant variables effecting protease production like rice husk (variable 1); inoculum size (variable 2); KNO3 (variable 3) have been identified under preliminary optimization studies. These variables are selected for a...

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...

Xenorhabdus luminescens Hm cultured in gelatin broth produced a single extracellular protease. The protease was purified by a factor of 500 and characterized as a monomeric protein with an approximate molecular weight of 61,000. On the basis of inhibitor studies and its pH optimum, the protease was classified as an alkaline metalloprotease with a pH optimum near 8; the isoelectric point of the ...