[Properties of chymotrypsin proteinase from Aspergillus oryzae].
Chymotrypsin-type proteinase is detected in the proteolytic system of Asp. oryzae. The action of it and chymotrypsin is shown to depend on formaldehyde. Hydrolysis of substrates, p-nitrophenyl acetate (p-NPA) and N-benzoyl-tyrosine methyl ether (BTME), by both preparations is almost the same. The obtained activity pH-optimum for the studied proteinase esterolytic activity is located in the alkaline zone as well as for crystalline chymotrypsin (substrate p-NPA). It concerns pH of both enzymes stability as well. The enzyme under study is relatively labile. At 50 degrees C there are only traces of the activity in the medium with p-NPG. Its considerable decrease is observed at 40 degrees C. This type activity is more stable on the substrate BTME. 10 min later it disappears completely in the enzymic preparation at a temperature of 60 degrees C at 40 degrees C it is 96.8%. For 24 h at 25 degrees C the activity lowers only by 8%. Crystalline chymotrypsin is stable under these conditions. DEAE-cellulose chromatography (different types of elution) detected multiple forms of proteinase differing in solubility chromatographic properties and specific activity when splitting the substrates p-NPA, BTME and casein.
D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D001549:Benzamides / Q000378:metabolism; D002364:Caseins / Q000378:metabolism; D002918:Chymotrypsin / Q000378:metabolism*; D004355:Drug Stability; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D005557:Formaldehyde / Q000494:pharmacology; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009578:Nitrobenzenes / Q000378:metabolism; D013329:Structure-Activity Relationship; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism
D001549:Benzamides; D002364:Caseins; D009578:Nitrobenzenes; D005557:Formaldehyde; D014443:Tyrosine; D010450:Endopeptidases; D002918:Chymotrypsin
Vlastivosti proteĭnazi khimotrpsinovogo tipu Aspergillus Oryzae.