A study on the comparative stability of insoluble complexes of glucose oxidase obtained with concanavalin A and specific polyclonal antibodies

• Published in: World journal of microbiology & biotechnology Vol. 22; no. 10; pp. 1033 - 1039
• Main Authors: JAN, Ulfat, AMJAD ALI KHAN, HUSAIN, Qayyum
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer 01-10-2006; Springer Nature B.V
• Subjects: Biological and medical sciences; Biosensors; Biotechnology; Enzymatic activity; Enzymes; Fundamental and applied biological sciences. Psychology; Glucose; Inactivation; Organic solvents; Polyclonal antibodies; Solvents; Urea; Glucose oxidase; Immunoglobulins; Stability; Enzyme; Antibody; Stabilization; cross-linked complexes; immuno-complexes; IgG; Immobilization; Crosslinking; immunoaffinity; Concanavalin A; Complexes; Oxidoreductases; Comparative study; insoluble complexes
• ISSN: 0959-3993; 1573-0972
• DOI: 10.1007/s11274-005-3208-6

The formation of insoluble complexes of glycoenzymes with lectins and antibodies is one of the simplest methods of enzyme immobilization. Insoluble complexes of glucose oxidase were simply obtained by mixing the enzyme with concanavalin A or a specific polyclonal antibodies solution. The concanavalin A and immunocomplexes of glucose oxidase retained more than 80% of the original enzyme activity. Expression of very high enzyme activity in insoluble complexes suggested that these aggregates were quite porous and easily accessible to substrates. Insoluble complexes of glucose oxidase showed very high stability against denaturation induced by pH, temperature, urea and water-miscible organic solvents. Complexes of glucose oxidase obtained with concanavalin A and glycosyl-specific antiglucose oxidase polyclonal antibodies were quite comparable in stability while complexes prepared using polyclonal antibodies raised against the native glucose oxidase were slightly less stable. The complexes of glucose oxidase obtained with glycosyl-specific antiglucose oxidase polyclonal antibodies showed very high stability against inactivation mediated by exposure to water-miscible organic solvents. Insoluble complexes of glucose oxidase were cross-linked with glutaraldehyde to maintain their integrity in the presence of substrates. The cross-linking of complexes resulted in a slight decrease in enzyme activity but showed a pronounced enhancement in stability against various forms of denaturation.[PUBLICATION ABSTRACT]