Co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase onto alkylamine glass beads through glutaraldehyde coupling

Abstract

A method for co-immobilizing lipase from porcine pancreas, glycerol kinase (GK) from <i>Cellulomonas </i>spp., glycerol-3-phosphate oxidase (GPO) from <i>Aerococcus viridans </i>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 <i>pH </i>and <i>Km </i>for triolein increased, while V_max 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

<span style="font-size:14.0pt;font-family:" times="" new="" roman";mso-fareast-font-family:="" "times="" roman";mso-ansi-language:en-us;mso-fareast-language:en-us;="" mso-bidi-language:ar-sa"="">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.</span>