Collect. Czech. Chem. Commun.
1990, 55, 841-845
https://doi.org/10.1135/cccc19900841
Extracellular proteinase from Brevibacterium linens. Purification and characterization
Ondrej Juhász, Danka Knošková, Jaroslav Zemanovič and Bohumil Škárka
Department of Technical Microbiology and Biochemistry, Slovak Technical University, 812 37 Bratislava
Abstract
Brevibacterium linens produces proteolytic enzymes in cultivation broth. One of them was purified by application of a two step procedure involving ultrafiltration and molecular sieving. The isolated enzyme hydrolyzed natural substrates: casein, hemoglobin, ovalbumin and bovine serum albumin with rations 22.2, 3.5, 1.6, 1.2 nkat mg-1, respectively. For casein the apparent Km 1.8 mg ml-1 was determined. The proteinase is fairly stable at pH 8.0 at 30 °C. Short term incubation at 50 °C denaturated the proteinase. SDS PAGE revealed an Mr of the proteolytic enzyme about 52 000 to 55 000.
