Immobilization Of Porcine Pancreatic Lipase Research Articles

Immobilization of porcine pancreatic lipase on glycidyl methacrylate grafted poly vinyl alcohol

Graft copolymerization of glycidyl methacrylate (GMA) on to polyvinyl alcohol (PVA) using benzophenone (BP) as initiator was carried out. Grafted PVA was used as carrier for pancreatic lipase immobilization. The effects of GMA and BP concentrations as well as grafting reaction times on grafting yields and activities of the immobilized lipase were determined. The influence of enzyme concentrations was also studied. The optimal conditions for the grafting reaction were: 1 h at 15 mM BP and 2.3 M GMA, the optimum enzyme concentration for immobilization was 1 mg/ml. After optimization of the immobilization process a physical and chemical characterization of the immobilized enzyme was performed. Furthermore, the thermal, pH, storage and operational stability of the immobilized enzyme in comparison to the free form was tested.

A novel enzyme support derived from aminated silica gel and polysuccinimide: preparation and application for the immobilization of porcine pancreatic lipase

A novel enzyme support was prepared by the reaction between the amine attached on silica gel and polysuccinimide. The capacity of polysuccinimide on silica gel was 0.131 g/g of support. The excess polysuccinimide in the reaction solution to prepare support could be recycled. This shows potential practicability for bulk preparation of the support. Porcine pancreatic lipase (PPL) was immobilized on the support with a high activity recovery. The residual PPL in immobilization solution still kept high activity and was recyclable for the further usage of immobilization. Compared to free PPL the stability of immobilized PPL against thermal and pH of reaction medium was significantly improved. It was found that the immobilized PPL stored at 37 °C in phosphate buffer could keep its activity for a long time, and had higher activity than the one stored in 4 °C.

Immobilization of porcine pancreatic lipase on celite for application in the synthesis of butyl butyrate in a nonaqueous system

AbstractFor immobilization of lipase, the use of a porous support material is recommended so that suitable amounts of lipase can be spread on a surface area without conformational changes. In this work, porcine pancreatic lipase was deposited on Celite, either by direct binding from aqueous solution or by deposition from aqueous solution by the addition of organic solvent. The influence of the immobilization procedure on the activities of the derivatives has been studied regarding their ability to synthesize butyl butyrate. The reaction rates were compared with the rate of esterification with free lipase. Better properties were displayed when the immobilized lipase form was prepared in an apolar solvent such as hexane. Under suitable reaction conditions, esterification yields as high as 90% were attained. Batch operational stability tests indicated that no enzyme deactivation occurs after 15 consecutive batches of 24 h each.

Covalent immobilization of porcine pancreatic lipase on amorphous AlPO4 and other inorganic supports

Porcine pancreatic lipase (PPL) was covalently immobilized through the formation of an aromatic Schiff's-base obtained by reaction of the ε-amino group of lysine residues in the enzyme and the aromatic aldehyde function of activated supports. The enzymatic activities of different immobilized PPL systems on amorphous AlPO4 and several inorganic supports at different pH values and temperatures were determined by hydrolysis of ethyl acetate. The nature of the support material critically affects the efficiency of enzyme immobilization as well as enzyme stability. All the supports examined, with the exceptions of cellulose and natural sepiolite, exhibited good properties for enzyme attachment. AlPO4 was the best support for enzyme immobilization, giving the highest percentage binding of enzyme (90%) and the highest retention of enzyme activity after immobilization (92·8%). © 1998 SCI

Covalent immobilization of porcine pancreatic lipase on amorphous AlPO4 and other inorganic supports

Porcine pancreatic lipase (PPL) was covalently immobilized through the formation of an aromatic Schiff's-base obtained by reaction of the ε-amino group of lysine residues in the enzyme and the aromatic aldehyde function of activated supports. The enzymatic activities of different immobilized PPL systems on amorphous AlPO4 and several inorganic supports at different pH values and temperatures were determined by hydrolysis of ethyl acetate. The nature of the support material critically affects the efficiency of enzyme immobilization as well as enzyme stability. All the supports examined, with the exceptions of cellulose and natural sepiolite, exhibited good properties for enzyme attachment. AlPO4 was the best support for enzyme immobilization, giving the highest percentage binding of enzyme (90%) and the highest retention of enzyme activity after immobilization (92·8%). © 1998 SCI

Immobilization of Porcine-Pancreatic Lipase on Silica Support to Study Lipolysis and Reverse Hydrolysis Reaction

Abstract Porcine-pancreatic lipase has been immobilized on epoxypropylsilanized PartiSphere-5. The hydrolysis of olive oil on this column provided oleic acid as the major reaction product. The reversal of the hydrolysis reaction was tested by esterification of acetic acid and benzoic acid under nonaqueous conditions.