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Enzyme Research
Volume 2014, Article ID 738739, 7 pages
http://dx.doi.org/10.1155/2014/738739
Research Article

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

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

Received 24 January 2014; Revised 24 March 2014; Accepted 24 March 2014; Published 10 April 2014

Academic Editor: Raffaele Porta

Copyright © 2014 Bárbara M. Bonine et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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.