PMID: 1199630Jan 1, 1975Paper

Comparison of the activities of free and carrier fixed horseradish peroxidase

Acta biologica et medica Germanica
D BaessK Ruckpaul

Abstract

Commerical horseradish-peroxidase was covalently bound to BrCN-activated sepharose. The activity parameters Vmax and Km were determined by the leukomalachite green reaction. Compared with the soluble enzyme, the immobilized POD has a relative residual activity of 22%. Dimethylsulfoxide and formamide were found to diminish the enzymatic activity in a concentration-dependent manner. The activity of the free enzyme in aqueous formamide solution (10%) is reduced by 43%, that of the insolubilized enzyme by 68%. Dimethylsulfoxide (15%) does not alter the LMG conversion rate of free POD, whilst a rate loss by 60% was observed for the immobilized enzyme.

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