Further characterization and kinetic parameter determination of a milk-clotting protease from Mucor bacilliformis.
Further characterization of an aspartyl protease from Mucor bacilliformis with milk-clotting activity was performed. An extinction coefficient, epsilon 278 cm = 1.61 mL/mg/cm, a molecular mass of 35,400 Da and a pI of 5.2 were determined. Proteolytic activity and kinetic parameters were evaluated by using the hexapeptide Leu-Ser-pNO2-Phe-Nle-Ala-Leu-OMe as the substrate. The effect of pH and temperature on peptide cleavage, as well as protease heat stability, was determined. Such properties, taken as a whole, indicate that the M. bacilliformis protease can be considered a potential substitute for bovine chymosin in cheese manufacture.
Venera
G D
GD
Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Facultad de Farmacía y Bioquímíca, Buenos Aires, Argentina.
Machalinski
C
C
Zumárraga
H
H
Biscoglio de Jiménez Bonino
M J
MJ
D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D002417:Cattle; D002611:Cheese; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007526:Isoelectric Point; D007700:Kinetics; D008892:Milk; D009089:Mucor / Q000201:enzymology*
D016282:Aspartic Acid Endopeptidases