Covalent immobilization of porcine pancreatic lipase on amorphous AlPO sub(4) and other inorganic supports

• Published in: Journal of chemical technology and biotechnology (1986) Vol. 72; no. 3; pp. 249 - 254
• Main Authors: Bautista, Felipa M, Bravo, Maria C, Campelo, Juan M, Garcia, Angel, Luna, Diego, Marinas, Jose M, Romero, Antonio A
• Format: Journal Article
• Language: English
• Published: 01-07-1998
• Subjects: Aldehydes; Aluminum compounds; Amorphous materials; Aromatic compounds; Catalyst activity; Catalyst supports; Chemical bonds; Hydrolysis; pH effects; Thermal effects
• ISSN: 0268-2575

Porcine pancreatic lipase (PPL) was covalently immobilized through the formation of an aromatic Schiff's-base obtained by reaction of the epsilon -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 AlPO sub(4) 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. AlPO sub(4) 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 times 8%).