Nov 1, 1975

Properties of penicillin amidase covalently bound to cellulose matrices

Antibiotiki
P S NysR I Fesenko

Abstract

Properties of penicillinamidase (PA) covalently bound with the cellulose matrix were studied. The efficiency of the binding depended on the bind type and purity of the native enzyme taken for binding. Stability of the immobilized PA (IPA) was studied at wide pH ranges. The effect of the ion strength, substrate concentration and purity of the native PA on stability of IPA was also investigated. The maximum stability of the enzyme was observed at pH 6.5-7.0 Stability of IPA depended on the purity of the native enzyme. When PA of the diazotized ether of cellulose containing amino groups was used, the enzyme was destabilized. IPA prepared on chlortriazinylcellulose was more stable than the respective native PA almost by I order.

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Mentioned in this Paper

Ions
Plasma Protein Binding Capacity
Enzyme Repression
Hydrogen-Ion Concentration
Enzyme Activation
Penicillin V Acylase
Amidohydrolases
Sulfite Cellulose

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