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- W22875701 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." @default.
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- W22875701 date "2002-10-01" @default.
- W22875701 modified "2023-09-26" @default.
- W22875701 title "Co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase onto alkylamine glass beads through glutaraldehyde coupling." @default.
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