Effects of the water-miscible organic solvents on lactoperoxidase purified from creek- XXXX milk.

@entity8694 @entity10977 @entity1042 @entity5723 @entity6188 @entity9104 @entity1626 @entity3733 @entity6442 @entity17114 @entity11520 @entity1068 @entity214
@entity11520 lactoperoxidase (WBLPO) was purified with Amberlite CG-50 ( @entity17114 form) resin, CM-Sephadex C-50 ion-exchange chromatography, and Sephadex G-100 gel-filtration chromatography from skimmed buffalo milk. The purity of the WBLPO was shown with @entity214 -PAGE. The R(z) (A(412)/A(280)) value for the WBLPO was 0.9. The optimum pH for the WBLPO was at 6.0. The K(m) value at optimum pH and 25 degrees C was 0.13 mM. The V(max) value at optimum pH and 25 degrees C was 5.3 micro mol/min per ml. The K(i) values for @entity1042 , @entity1068 , @entity3733 ( @entity3733 ), @entity1626 , @entity5723 , @entity6188 ( @entity8694 ), @entity6442 ( @entity9104 ), and @entity10977 were 1.087, 0.364, 0.302, 0.459, 0.330, 0.126, 0.093, and 2.125 M, respectively. All the solvents showed competitive inhibition. The I(50) values of @entity1042 , @entity1068 , @entity3733 , @entity1626 , @entity5723 , @entity6188 , @entity6442 , and @entity10977 were 2.910, 0.942, 0.537, 1.320, 0.875, 0.470, 0.405, and 3.920 M, respectively. @entity10977 , @entity1042 , @entity1626 , and @entity1068 have been found to be very promising solvents for performing biocatalytic reactions with LPO in organic media.
