3.4.21.64: peptidase K

proteinase K and Cu2+ ions are used to synthesize enzyme-inorganic hybrid nanoflowers (P-hNFs). The P-hNFs exhibit better activity than free proteinase K in the presence of all surfactants, i.e. CHAPS, DOC, SDS, Triton X-100 and Tergitol, except for Tween 80. synthesized enzyme-inorganic hybrid nanoflowers (P-hNFs) can potentially be used as an additive in detergent formulations

753849

dysprosium

1 mM DyCl3, differential scanning calorimetry analysis bound to the enzyme

europium

1 mM EuCl33, differential scanning calorimetry analysis bound to the enzyme

gadolinium

1 mM GdCl33, differential scanning calorimetry analysis bound to the enzyme

holmium

1 mM HoCl3, differential scanning calorimetry analysis bound to the enzyme

lanthanum

1 mM La(NO3)3, differential scanning calorimetry analysis bound to the enzyme

lutetium

1 mM LuCl3, differential scanning calorimetry analysis bound to the enzyme

neodymium

1 mM NdCl3, differential scanning calorimetry analysis bound to the enzyme

Pr3+

1 mM PrCl3, the denaturation temperature of proteinase K derivatized with praseodymium (Pr) ions is 16.2°C, which is 5.9°C higher than those of metal-free and Ca2+-bound proteinase K, respectively. Isothermal titration calorimetry (ITC) measurements demonstrate that Pr-ion binding to proteinase K shows endothermic peaks, whereas Ca2+-ion binding shows exothermic peaks, indicating that the binding mode of Pr ions is different from that of Ca2+ ions, even though the crystal structures of proteinase K with Pr and Ca2+ ions are identical. Hydrolytic activity of Pr-derivatized proteinase K shows that the hydrolytic activity is 46fold higher at 70°C using synthetic nitroanilide substrate and 9 and 76fold higher at 70°C and 80°C using fluorescein isothiocyanate-labeled casein, respectively, in comparison with the native proteinase K. Furthermore, based on the yield of chemoenzymatic peptide syntheses, the aminolysis activity of Pr-derivatized proteinase K is 3.5 and 9.5fold higher than that of the native proteinase K at 50°C and 60°C, respectively. Analysis of the mechanism by which Pr ions enhance the thermal stability of proteinase K, overview

samarium

1 mM SmCl3, differential scanning calorimetry analysis bound to the enzyme

SDS

stimulates hydrolysis of serum albumin in a dose-dependent manner, caused primarily by denaturation of the protein substrate, inactivates with an oligopeptide as substrate

29506

Urea

stimulates hydrolysis of serum albumin in a dose-dependent manner, caused primarily by denaturation of the protein substrate

29506

ytterbium

1 mM YbCl3, differential scanning calorimetry analysis bound to the enzyme

additional information

differential scanning calorimetry curves for proteinase K derivatized with heavy atoms, showing the correlation between atomic number and denaturation temperature, overview