[Stableness of the alkaline protease of the fungus Torula thermophila strain UzPT-1 to heating and the action of Ca2+ ions].
Thermal stability of protease of the fungus Torula thermophila strain UzPT-1 was examined. The dependence of this property on the content of monomer and dimer forms in the preparation was also investigated. The preparations with a high content of the dimer form showed greater thermal stability in distilled water. The preparations/with the predominant monomer from retained thermal stability in buffer solutions at pH 8 and lost it in distilled water when stored in the cold (2-4 degrees C) for several days. The preparations which lost thermal stability upon ammonium sulphate precipitation recovered partially or completely after addition of Ca2+ ions at a concentration of 0.001 M.
D002118:Calcium / Q000494:pharmacology*; D002413:Cations, Divalent; D002850:Chromatography, Gel; D003454:Cryptococcus / Q000201:enzymology*; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology*; D012996:Solutions; D013696:Temperature
D002413:Cations, Divalent; D012996:Solutions; D010447:Peptide Hydrolases; D002118:Calcium
Ustoĭchivost' shchelochnoĭ proteazy griba Torula thermophila shtamm UzPT-1 nagrevaniiu, deĭstvie ionov Ca2+