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Enzyme Res. 2014;2014:738739. doi: 10.1155/2014/738739. Epub 2014 Apr 10.

Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads.

Enzyme research

Bárbara M Bonine, Patricia Peres Polizelli, Gustavo O Bonilla-Rodriguez

Affiliations

  1. Department of Chemistry and Environmental Sciences, Universidade Estadual Paulista, IBILCE-UNESP, Rua Cristovão Colombo 2265, 15054-000 São José do Rio Preto, SP, Brazil.
  2. Department of Pharmacy and Biochemistry, Centro Universitário de Rio Preto, UNIRP, Rua Ivete Gabriel Atique 45, 15025-400 São José do Rio Preto, SP, Brazil.

PMID: 24818012 PMCID: PMC4003796 DOI: 10.1155/2014/738739

Abstract

This study reports the immobilization of a new lipase isolated from oleaginous seeds of Pachira aquatica, using beads of calcium alginate (Alg) and poly(vinyl alcohol) (PVA). We evaluated the morphology, number of cycles of reuse, optimum temperature, and temperature stability of both immobilization methods compared to the free enzyme. The immobilized enzymes were more stable than the free enzyme, keeping 60% of the original activity after 4 h at 50°C. The immobilized lipase was reused several times, with activity decreasing to approximately 50% after 5 cycles. Both the free and immobilized enzymes were found to be optimally active between 30 and 40°C.

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