title: [Various physico-chemical properties of lytic proteinase L2 of the enzyme preparation lysoamidase isolated from bacteria of Pseudomonadaceae family].
abstract: Some physico-chemical properties of lytic proteinase L2 isolated from the enzymatic microbial preparation of lysoamidase were studied. The molecular mass of the enzyme is 15 000 Da, pI is 5.3. The enzyme hydrolyzes casein as well as the cells and cell walls of Staphylococcus aureus 209-P. The pH optimum of casein hydrolysis lies at 9.5; that for cell wall hydrolysis at 8.0. The temperature optimum for casein hydrolysis and cell lysis lies at 55 degrees C and 65 degrees C, respectively. The enzyme proteolytic activity is inhibited by serine proteinase inhibitors in a greater degree than the lytic activity. 50% of the proteolytic and lytic activities is lost upon enzyme heating for 15 min at 65 degrees C.
mesh_terms: D001433:Bacteriolysis; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification*; D006868:Hydrolysis; D007526:Isoelectric Point; D011480:Protease Inhibitors; D011548:Pseudomonadaceae / Q000201:enzymology*; D012697:Serine Endopeptidases
chemical_list: D011480:Protease Inhibitors; D010450:Endopeptidases; D012697:Serine Endopeptidases
vernacular_title: Nekotorye fiziko-khimicheskie svoĭstva liticheskoĭ proteinazy L2 fermentnogo preparata lizoamidazy, vydelennogo iz bakterii semeĭstva Pseudomonadaceae.