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Immobilization of lipase from Candida rugosa on Eupergit® C supports by covalent attachment

✍ Scribed by Zorica Knezevic; Nenad Milosavic; Dejan Bezbradica; Zivana Jakovljevic; Radivoje Prodanovic

Publisher
Elsevier Science
Year
2006
Tongue
English
Weight
202 KB
Volume
30
Category
Article
ISSN
1369-703X

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## Abstract **BACKGROUND:** Immobilization of lipase (triacylglycerol acylhydrolase EC 3.1.1.3) from __Candida rugosa__ on Eupergit^®^ C and Eupergit^®^ C 250L was performed under microwave irradiation in order to reduce immobilization time. Lipase loading, hydrolytic activity, esterification activ

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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 sy