Formation and properties of horseradish peroxidase colloidal clusters.

Citation:

Kamyshny A, Reuveni T, Magdassi S. Formation and properties of horseradish peroxidase colloidal clusters. J. Colloid Interface Sci.Journal of Colloid and Interface Science. 1996;181 (2) :470 - 475.

Date Published:

1996///

Abstract:

Hydrophobic modification of horseradish peroxidase by fatty acid esters (C8, C12, C16, C18) of N-hydroxysuccinimide was carried out. The degree of modification increases with an increase in the ester:enzyme molar ratio and reaches a maximal value of four modified amino groups when this ratio is 150:1. Covalent attachment of hydrophobic groups to the peroxidase mols. leads to a spontaneous formation of micelle-like colloidal clusters, which have a mean diam. of 65 nm at the maximal degree of modification by C16-ester. The fraction of the enzyme mols. which forms clusters depends on both the length of the attached hydrophobic chain and the degree of modification. The colloidal clusters, which are composed of the modified peroxidase, have about 80 and 50% lower enzymic activities for C12- and C16- modified enzymes. [on SciFinder(R)]