Resistance to deactivation of enzyme-collagen membranes.
Amongst the attractive properties of immobilized enzymes, an enhanced stability is very often underlined. In our case, the covalent attachment of numerous enzymes from different classes to water-insoluble collagen films allowed us to study their resistance to inactivation or denaturation after coupling. The influence of heat, denaturing reagents like concentrated urea or guanidinium chloride, the incubation in the presence of glutaraldehyde, have been tested on aspartate amino-transferase either in soluble form or bound on collagen films. The fact that diffusional effects can lead to an apparent enhancement of stability after immobilization has been taken into account and their influence studied for both thermal and storage stability : diffusional limitations are partly responsible for the enhanced stability of the bound enzyme but the binding to the collagen membrane itself increases its storage stability. The resistance of proteolytic enzymes to autolysis has also been checked.
D001219:Aspartate Aminotransferases; D003094:Collagen; D004800:Enzymes, Immobilized; D005976:Glutaral; D019791:Guanidine; D006146:Guanidines; D008567:Membranes, Artificial; D011489:Protein Denaturation; D013696:Temperature; D013997:Time Factors; D014508:Urea
D004800:Enzymes, Immobilized; D006146:Guanidines; D008567:Membranes, Artificial; D014508:Urea; D003094:Collagen; D001219:Aspartate Aminotransferases; D019791:Guanidine; D005976:Glutaral