Volume 11, Issue 3 p. 266-272

Characterization of free and immobilized amine oxidases

R. Stevanato

R. Stevanato

Department of Physical Chemistry, University of Venice, Italy.

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M. Porchia

M. Porchia

Department of Physical Chemistry, University of Venice, Italy.

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O. Befani

O. Befani

Department of Physical Chemistry, University of Venice, Italy.

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B. Mondovi

B. Mondovi

Department of Physical Chemistry, University of Venice, Italy.

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A. Rigo

A. Rigo

Department of Physical Chemistry, University of Venice, Italy.

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First published: June 1989
Citations: 2

Abstract

Bovine plasma amine oxidase was covalently bound to CH-Sepharose 4B by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride. The immobilized enzyme showed no significant change in specific activity when spermidine was the substrate, while the enzyme affinity toward benzylamine and propylamine increased significantly. Similarly, the pig kidney diamine oxidase physically adsorbed to Con A-Sepharose showed large changes in affinity toward substrates such as p-dimethylaminoethylbenzylamine with respect to the native enzyme. These changes are discussed in terms of active site modification as a consequence of the enzyme immobilization.