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

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...

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Detalles Bibliográficos
Autores principales: Bonine, Bárbara M., Polizelli, Patricia Peres, Bonilla-Rodriguez, Gustavo O.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4003796/
https://www.ncbi.nlm.nih.gov/pubmed/24818012
http://dx.doi.org/10.1155/2014/738739
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author Bonine, Bárbara M.
Polizelli, Patricia Peres
Bonilla-Rodriguez, Gustavo O.
author_facet Bonine, Bárbara M.
Polizelli, Patricia Peres
Bonilla-Rodriguez, Gustavo O.
author_sort Bonine, Bárbara M.
collection PubMed
description 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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spelling pubmed-40037962014-05-11 Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads Bonine, Bárbara M. Polizelli, Patricia Peres Bonilla-Rodriguez, Gustavo O. Enzyme Res Research Article 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. Hindawi Publishing Corporation 2014 2014-04-10 /pmc/articles/PMC4003796/ /pubmed/24818012 http://dx.doi.org/10.1155/2014/738739 Text en Copyright © 2014 Bárbara M. Bonine et al. https://creativecommons.org/licenses/by/3.0/ 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.
spellingShingle Research Article
Bonine, Bárbara M.
Polizelli, Patricia Peres
Bonilla-Rodriguez, Gustavo O.
Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads
title Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads
title_full Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads
title_fullStr Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads
title_full_unstemmed Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads
title_short Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads
title_sort immobilization of a plant lipase from pachira aquatica in alginate and alginate/pva beads
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4003796/
https://www.ncbi.nlm.nih.gov/pubmed/24818012
http://dx.doi.org/10.1155/2014/738739
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