MODIFICATION OF ENZYME PROPERTIES BY THE USE OF INHIBITORS DURING THEIR STABILIZATION BY MULTIPOINT COVALENT ATTACHMENT

The effect of a number of inhibitors adsorbed at the active site of pe nicillin acylase during immobilisation/stabilisation is reported. Each inhibitor, when it is adsorbed at the active centre of penicillin acy lase promotes a specific enzymatic conformation which remains fixed af ter the stabilisation process by multipoint covalent attachment to pre -existing supports. A number of inhibitors: penicillin sulfoxide, phen ylacetic acid, mandelic acid, and phenylglycine were employed to induc e conformational changes. The activity towards different substrates of the enzyme derivative (in hydrolysis and in synthesis) was determined . The stability of the derivatives was also measured. This technique p rovides a broad spectrum of enzymatic derivatives with a range of acti vity/stability depending on the inhibitors used in their stabilisation . The resulting choice offers a considerably increased potential for t he use of the enzyme since one can select a derivative which will spec ifically catalyse the reaction of interest.