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Immobilization of Candida Rugosa Lipase on Magnetized Dacron: Kinetic Study

Immobilization of Candida Rugosa Lipase on Magnetized Dacron: Kinetic Study

M C B Pimentel, A B F Leāo, E H M Melo, W M Ledingham, J L Lima Filho, M Sivewright, J F Kennedy

Artif Cells Blood Substit Immobil Biotechnol. 2007;35(2):221-35.

PMID: 17453706

Abstract:

Candida rugosa lipase has been covalently immobilized on ferromagnetic azide polyethyleneterepthalate (Dacron) with specific activity retention of 16% for 4-nitrophenyl palmitate and 24% for hydrolysis of triolein in hexane. The immobilized enzyme was more thermal stable than the soluble one, retaining 78.8% of the activity after 1 h at 60 degrees C. Also, this immobilized derivative was stable at the storage at 4 degrees C. It has been used 5 cycles for pNPP hydrolysis without loss of activity. Soluble and immobilized Candida rugosa lipase showed a Michaelian behavior for fatty acid 4-nitrophenyl esters and different apparent K(M) values: 0.110 mM and 0.124 mM (4-nitrophenyl palmitate - C16); 0.193 mM and 0.235 mM (4-nitrophenyl laurate - C12) and 0.206 mM and 0.119 mM (4-nitrophenyl butyrate - C4), respectively. The immobilized lipase was more efficient for catalyzing the hydrolysis of 4-nitrophenyl esters with short chain length fatty acid (4-NPB - C4) than soluble enzyme. The ferromagnetic Dacron-lipase derivative was able to catalyze the synthesis of triolein from glycerol and oleic acid with 50% of conversion after 72 h at 40 degrees C.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP2635849	4-Nitrophenyl butyrate		2635-84-9	Price

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