[Proteolytic resistance and thermostability of catalase and histidine decarboxylase from Micrococcus sp. n].
Catalase from Micrococcus sp. n. is not hydrolyzed by trypsin at the protein/protease (pn/pe) exceeding 10/1. Histidine decarboxylase (HDC) loses 50% of activity after the first nine minutes of hydrolysis at the pn/pe ratio equal to 6/1, followed by a slow linear inactivation. Investigation of thermal stability at varying pH and temperatures demonstrated that catalase and HDC preserve 70-80% of activity after 5 minutes of incubation at 72 degrees C only at pH approaching the optimal pH of enzymatic activity (pH 7.45 for catalase and pH 5.55 for HDC).
D002262:Carboxy-Lyases / Q000378:metabolism*; D002374:Catalase / Q000378:metabolism*; D006640:Histidine Decarboxylase / Q000378:metabolism*; D006358:Hot Temperature; D006868:Hydrolysis; D008837:Micrococcus / Q000201:enzymology*; D014357:Trypsin
D002374:Catalase; D014357:Trypsin; D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase
Proteoliticheskaia ustoĭchivost' i termostabil'nost' katalazy i gistidindekarboksilazy iz Micrococcus sp. n.