Please use this identifier to cite or link to this item:
|Title:||Co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase onto alkylamine glass beads through glutaraldehyde coupling|
Pundir, C S
|Abstract:||A method for co-immobilizing lipase from porcine pancreas, glycerol kinase (GK) from Cellulomonas spp., glycerol-3-phosphate oxidase (GPO) from Aerococcus viridans and peroxidase from horseradish onto zirconia-coated alkylamine glass beads through glutaraldehyde coupling has been described. The co-immobilized enzymes retained 71.4% of initial specific activity with a conjugation yield of 43.6 mg/g support. The optimum pH and Km for triolein increased, while Vmax was decreased slightly, but incubation temperature for maximum activity remained unaltered after co-immobilization. The co-immobilized enzymes showed increased thermal and storage stabilities in cold, compared to their native form. Among the various metal salts tested, only CuSO4 caused inhibition of both free and co-immobilized enzymes. The co-immobilized enzymes showed better suitability over mixture of individually immobilized enzymes in determination of serum triglyceride.|
|ISSN:||0975-0959 (Online); 0301-1208 (Print)|
|Appears in Collections:||IJBB Vol.39(5) [October 2002]|
Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.