Effect of immobilization protocol on optimal conditions of ethyl butyrate synthesis catalyzed by lipase B from Candida antarctica

Authors

  • John L. R. Friedrich,

    1. Biocatalysis and Enzyme Technology Lab, Institute of Food Science and Technology, Federal University of Rio Grande do Sul State, Porto Alegre, RS, Brazil
    Search for more papers by this author
  • Fernanda P. Peña,

    1. Biocatalysis and Enzyme Technology Lab, Institute of Food Science and Technology, Federal University of Rio Grande do Sul State, Porto Alegre, RS, Brazil
    Search for more papers by this author
  • Cristina Garcia-Galan,

    1. Department of Biocatalysis, ICP – CSIC, Campus UAM-CSIC, Cantoblanco, Madrid, Spain
    Search for more papers by this author
  • Roberto Fernandez-Lafuente,

    1. Department of Biocatalysis, ICP – CSIC, Campus UAM-CSIC, Cantoblanco, Madrid, Spain
    Search for more papers by this author
  • Marco A. Z. Ayub,

    1. Biochemical Engineering Lab (BiotecLab), Institute of Food Science and Technology, Federal University of Rio Grande do Sul State, Porto Alegre, RS, Brazil
    Search for more papers by this author
  • Rafael C. Rodrigues

    Corresponding author
    • Biocatalysis and Enzyme Technology Lab, Institute of Food Science and Technology, Federal University of Rio Grande do Sul State, Porto Alegre, RS, Brazil
    Search for more papers by this author

Correspondence to: R.C. Rodrigues,

Biocatalysis and Enzyme Technology Lab, Institute of Food Science and Technology,

Federal University of Rio Grande do Sul State, Av

Bento Gonçalves, 9500, P.O. Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil.

E-mail: rafaelcrodrigues@ufrgs.br

Abstract

Background

In this work two immobilized preparations of lipase (EC 3.1.1.3) B from Candida antarctica (CALB) were compared as biocatalysts in the synthesis of ethyl butyrate, a short-chain esters with fruity notes. Commercial Novozym 435 and CALB immobilized on styrene-divinylbenzene beads (MCI-CALB) were tested for esterification reactions. Central composite design and response surface methodology were used to optimize the reaction temperature, substrate molar ratio, enzyme content, and the added water.

Results

The two enzymatic preparations presented different optimal conditions concerning ethyl butyrate production, with higher yields of conversion around 85% in 1.5 h being achieved. However, MCI-CALB presented productivities 1.6 times higher than Novozym 435. The main difference between the biocatalysts was in relation to operational stability during batch reuse experiments, in which MCI-CALB retained 80% of its initial activity after eight batches, while Novozym 435 retained only 20% under the same conditions.

Conclusion

It was verified that variations in the protocols for enzyme immobilization causes different optimal conditions for the esterification reaction. These are very interesting results because reaction times were short, producing high conversion yields and productivities considering the mass of biocatalyst used. © 2012 Society of Chemical Industry

Ancillary