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Effect of Support Pore Size on Activity of Immobilized Sulfhydryl Oxidase¹

Department of Food Science, North Carolina State University, Raleigh, North Carolina 27607

ABSTRACT

Both sulfhydryl oxidase and heat denatured milk proteins exist as highly associated, large protein complexes; therefore, the catalytic activity of immobilized forms of the enzyme should be dependent upon the pore size of the support matrix. A method was optimized for immobilization of the enzyme on succinamidopropyl-glass with water-soluble carbodiimide to activate carboxyl groups. With both heated skim milk and reduced glutathione substrates most of the activity occurred on the outer surface of the particles for enzyme immobilized on porous beads having mean pore diameters ranging from 500 A to 3000 A. Furthermore, Arrhenius plots did not indicate significant effects of pore diffusion. Also molecular sieve chromatographic experiments showed that enzyme and denatured whey proteins were excluded from the pore volume. Finally, equivalent or higher activity per unit volume of support could be obtained with nonporous materials such as glass beads.

¹ Paper No. 5462 of the Journal Series of the North Carolina Agricultural Experiment Station, Raleigh, 27607. This study was supported partially by the Research Applied to National Needs Program, National Science Foundation, Grant APR 73-07877 A01. Any opinions, findings, conclusions, or recommendations expressed in this publication are those of the authors and do not reflect necessarily the views of the National Science Foundation. The use of trade names in this publication does not imply endorsement by the North Carolina Agricultural Experiment Station of the products.