Studies on the heat inactivation of porcine kidney aminoacylase.
Heat inactivation of porcine kidney aminoacylase (E.C.3.5.1.14) was investigated under different conditions i.e. at different temperatures, protein concentrations and pH values). Kinetic analysis of the inactivation process suggests that aminoacylase is a dissociable enzyme: the dimeric form is dissociated to enzymatically active monomers and the heat stability of the dimer is higher than that of the monomers. High temperatures, dilution and pH values other than neutral, all promote dissociation. The KDapp at 60 degrees C, pH 7.0 is of the order of 10(-6) M.
D000581:Amidohydrolases / Q000032:analysis*; D000818:Animals; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D010446:Peptide Fragments / Q000032:analysis; D011489:Protein Denaturation; D013552:Swine
D010446:Peptide Fragments; D000581:Amidohydrolases; C019672:aminoacylase I