Covalent immobilization of porcine pancreatic lipase on amorphous AlPO4 and other inorganic supports
✍ Scribed by Felipa M. Bautista; Maria C. Bravo; Juan M. Campelo; Angel García; Diego Luna; José M. Marinas; Antonio A. Romero
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1998
- Tongue
- English
- Weight
- 209 KB
- Volume
- 72
- Category
- Article
- ISSN
- 0268-2575
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✦ Synopsis
Porcine pancreatic lipase (PPL) was covalently immobilized through the formation of an aromatic Schi † Ïs-base obtained by reaction of the e-amino group of lysine residues in the enzyme and the aromatic aldehyde function of activated supports. The enzymatic activities of di †erent immobilized PPL systems on amorphous and several inorganic supports at di †erent pH AlPO 4 values and temperatures were determined by hydrolysis of ethyl acetate. The nature of the support material critically a †ects 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.
was the best support for enzyme immobilization, giving the AlPO 4 highest percentage binding of enzyme (90%) and the highest retention of enzyme activity after immobilization (92É8%).
1998 SCI (