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Some properties of a papain–agarose reactor provided with a pH monitor by L. A. Ae. Sluyterman; J. Wijdenes is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract A small reactor of immobilized papain was used to gain some knowledge about the effect of immobilization upon the reactivity of the enzyme towards one substrate and various types of inhibitors. A buffer solution containing benzoyl–arginine ethyl ester as substrate was run through a small column of papain immobilized by attachment to agarose beads. The pH of the effluent was measured continuously and provided the data used to calculate the substrate conversion during passage through the reactor. The operation of the system was checked by determining the substrate conversion as a function of flow rate. It proved to operate as theory demanded. The rate and extent of inhibition were measured after addition of various inhibitors to the buffer–substrate solution. The following quantities of immobilized papain were found to be equal within ±20% to those of the free enzyme in solution: the overall activity, the __K__~__m__~ of benzoyl–arginine ethyl ester, the __K__~__i__~ of the competitive inhibitor benzoylamino‐acetonitrile, the rate of inactivation by chloroacetic acid and by chloroacetamide, the rate of activation by cysteine of the mixed disulfide of papain and cysteine,

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Author

L. A. Ae. Sluyterman; J. Wijdenes

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley - V C H Verlag GmbbH & Co.; Wiley (ISSN 0006-3592)

Published

1981

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)