Covalent immobilization of invertase and horseradish peroxidase on concanavalin A-Seralose via carbohydrate moieties.
Invertase from Baker's yeast (Saccharomyces cerevisiae) and Horseradish peroxidase (HRP) were covalently immobilized on Concanavalin A precoupled to Seralose via carbohydrate moieties. Covalent coupling of glycoenzymes was achieved by periodate induced aldehydic groups of glycosyls with amino groups of Concanavalin A, at different pH values. A bifunctional reagent such as glutaraldehyde crosslinks the glycoenzymes with lectin both intra and intermolecularly. Therefore, attempts were made to introduce covalent linkages between glycoenzymes and Concanavalin A-Seralose without intramolecular crosslinking in either. The immobilized preparations of glycoenzymes exhibited high yield of immobilization and eta value. About 90 and 85% covalent coupling could be observed in invertase and HRP at pH 7.0 respectively, as determined by treatment with 0.5 M methyl alpha-D-mannopyranoside. All immobilized glycoenzyme preparations exhibited marked stabilization towards thermal inactivation.
Husain
S
S
Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, India.
Jafri
F
F
D002241:Carbohydrates; D003208:Concanavalin A; D004800:Enzymes, Immobilized; D006026:Glycoside Hydrolases; D006863:Hydrogen-Ion Concentration; D009195:Peroxidase; D037121:Plant Lectins; D010944:Plants / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D043324:beta-Fructofuranosidase
D002241:Carbohydrates; D004800:Enzymes, Immobilized; D037121:Plant Lectins; D003208:Concanavalin A; D009195:Peroxidase; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase