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Further Stabilization of Lipase From Pseudomonas Fluorescens Immobilized on Octyl Coated Nanoparticles via Chemical Modification With Bifunctional Agents

Further Stabilization of Lipase From Pseudomonas Fluorescens Immobilized on Octyl Coated Nanoparticles via Chemical Modification With Bifunctional Agents

Nathalia Saraiva Rios, Eva Gomes Morais, Wesley Dos Santos Galvão, Davino M Andrade Neto, José Cleiton Sousa Dos Santos, Felipe Bohn, Marcio A Correa, Pierre Basílio Almeida Fechine, Roberto Fernandez-Lafuente, etc.

Int J Biol Macromol. 2019 Dec 1;141:313-324.

PMID: 31491511

Abstract:

The lipase from Pseudomonas fluorescens (PFL) was adsorbed on superparamagnetic NiZnFe2O4 octyl-nanoparticles via interfacial activation, producing the biocatalyst OCTYL-NANO-PFL. In order to further improve the stability of the immobilized lipase, the immobilized enzyme biocatalyst was chemically modified with different concentrations of diverse bifunctional molecules (glutaraldehyde (GA), divinylsulfone (DVS) or p-benzoquinone (BQ)). The concentrations of bifunctional agents were varied (0.5, 1, 2.5 and 5% (v/v for GA and DVS and w/v for BQ)). The results showed a greatly improved stability after chemical modification with all bifunctional molecules, mainly with 5% (v/v) GA or 1% (v/v) DVS. The biocatalysts OCTYL-NANO-PFL-GA 5% and -DVS 1% were about 60 folds more stable at pH 7 than the unmodified preparation and, at pH 5, >200 folds for 5% GA modified enzyme. The most stable BQ treated biocatalysts, OCTYL-NANO-PFL-BQ 0.5%, was about 8.3 more stable than OCTYL-NANO-PFL at pH 7, while was 20 fold more stable at pH 9.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42415164	Lipase, immobilized in Sol-Gel-AK, from Pseudomonas fluorescens			Price

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