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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2014
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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. |
format | Online Article Text |
id | pubmed-4003796 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
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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