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Carrier-free Immobilization of Lipase From Candida Rugosa With Polyethyleneimines by Carboxyl-Activated Cross-Linking

Carrier-free Immobilization of Lipase From Candida Rugosa With Polyethyleneimines by Carboxyl-Activated Cross-Linking

Susana Velasco-Lozano, Fernando López-Gallego, Rafael Vázquez-Duhalt, Juan C Mateos-Díaz, José M Guisán, Ernesto Favela-Torres

Biomacromolecules. 2014 May 12;15(5):1896-903.

PMID: 24720524

Abstract:

Carrier-free immobilization of Candida rugosa lipase (CRL) and polymers containing primary amino groups were cross-linked using carbodiimide. To accomplish this, the free carboxyl groups of the enzyme were activated with carbodiimide-succinimide in organic medium, and then the activated proteins were cross-linked with different polyethylenimines (PEIs). The effect of the cross-linker chain length, the amount of added bovine serum albumin (BSA), and carbodiimide concentration on the catalytic properties of resulting cross-linked enzyme aggregates (CLEAs) was investigated. The CLEAs' size, shape, specific activity, activity recovery, thermostability and enantioselectivity significantly varied according to the preparation procedure. The highest thermostable CRL-CLEA preparation was obtained with 1.3 kDa polyethyleneimine as cross-linker, 10 mg of BSA and 28 mM of carbodiimide. This preparation is 1.3-fold more active and thermostable than CLEAs prepared by the traditional method of amino cross-linking with glutaraldehyde, and retains 60% of residual activity after 22 h at 50 °C. Additionally, the CRL-CLEA preparation showed an enantioselectivity of 91% enantiomeric excess (ee). This immobilization procedure provides an alternative strategy for CLEA production, particularly for enzymes where the traditional method of cross-linking via lysine residues leads to enzyme inactivation.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416030	Lipase, Candida rugosa, CLEA			Price

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