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Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases
A commercial and very hydrophobic styrene-divinylbenzene matrix, MCI GEL(®) CHP20P, has been compared to octyl-Sepharose(®) beads as support to immobilize three different enzymes: lipases from Thermomyces lanuginosus (TLL) and from Rhizomucor miehie (RML) and Lecitase(®) Ultra, a commercial artifici...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6271320/ https://www.ncbi.nlm.nih.gov/pubmed/24918537 http://dx.doi.org/10.3390/molecules19067629 |
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author | Garcia-Galan, Cristina Barbosa, Oveimar Hernandez, Karel dos Santos, Jose C. S. Rodrigues, Rafael C. Fernandez-Lafuente, Roberto |
author_facet | Garcia-Galan, Cristina Barbosa, Oveimar Hernandez, Karel dos Santos, Jose C. S. Rodrigues, Rafael C. Fernandez-Lafuente, Roberto |
author_sort | Garcia-Galan, Cristina |
collection | PubMed |
description | A commercial and very hydrophobic styrene-divinylbenzene matrix, MCI GEL(®) CHP20P, has been compared to octyl-Sepharose(®) beads as support to immobilize three different enzymes: lipases from Thermomyces lanuginosus (TLL) and from Rhizomucor miehie (RML) and Lecitase(®) Ultra, a commercial artificial phospholipase. The immobilization mechanism on both supports was similar: interfacial activation of the enzymes versus the hydrophobic surface of the supports. Immobilization rate and loading capacity is much higher using MCI GEL(®) CHP20P compared to octyl-Sepharose(®) (87.2 mg protein/g of support using TLL, 310 mg/g using RML and 180 mg/g using Lecitase(®) Ultra). The thermal stability of all new preparations is much lower than that of the standard octyl-Sepharose(®) immobilized preparations, while the opposite occurs when the inactivations were performed in the presence of organic co-solvents. Regarding the hydrolytic activities, the results were strongly dependent on the substrate and pH of measurement. Octyl-Sepharose(®) immobilized enzymes were more active versus p-NPB than the enzymes immobilized on MCI GEL(®) CHP20P, while RML became 700-fold less active versus methyl phenylacetate. Thus, the immobilization of a lipase on this matrix needs to be empirically evaluated, since it may present very positive effects in some cases while in other cases it may have very negative ones. |
format | Online Article Text |
id | pubmed-6271320 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62713202018-12-21 Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases Garcia-Galan, Cristina Barbosa, Oveimar Hernandez, Karel dos Santos, Jose C. S. Rodrigues, Rafael C. Fernandez-Lafuente, Roberto Molecules Article A commercial and very hydrophobic styrene-divinylbenzene matrix, MCI GEL(®) CHP20P, has been compared to octyl-Sepharose(®) beads as support to immobilize three different enzymes: lipases from Thermomyces lanuginosus (TLL) and from Rhizomucor miehie (RML) and Lecitase(®) Ultra, a commercial artificial phospholipase. The immobilization mechanism on both supports was similar: interfacial activation of the enzymes versus the hydrophobic surface of the supports. Immobilization rate and loading capacity is much higher using MCI GEL(®) CHP20P compared to octyl-Sepharose(®) (87.2 mg protein/g of support using TLL, 310 mg/g using RML and 180 mg/g using Lecitase(®) Ultra). The thermal stability of all new preparations is much lower than that of the standard octyl-Sepharose(®) immobilized preparations, while the opposite occurs when the inactivations were performed in the presence of organic co-solvents. Regarding the hydrolytic activities, the results were strongly dependent on the substrate and pH of measurement. Octyl-Sepharose(®) immobilized enzymes were more active versus p-NPB than the enzymes immobilized on MCI GEL(®) CHP20P, while RML became 700-fold less active versus methyl phenylacetate. Thus, the immobilization of a lipase on this matrix needs to be empirically evaluated, since it may present very positive effects in some cases while in other cases it may have very negative ones. MDPI 2014-06-10 /pmc/articles/PMC6271320/ /pubmed/24918537 http://dx.doi.org/10.3390/molecules19067629 Text en © 2014 by the authors. licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Garcia-Galan, Cristina Barbosa, Oveimar Hernandez, Karel dos Santos, Jose C. S. Rodrigues, Rafael C. Fernandez-Lafuente, Roberto Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases |
title | Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases |
title_full | Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases |
title_fullStr | Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases |
title_full_unstemmed | Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases |
title_short | Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases |
title_sort | evaluation of styrene-divinylbenzene beads as a support to immobilize lipases |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6271320/ https://www.ncbi.nlm.nih.gov/pubmed/24918537 http://dx.doi.org/10.3390/molecules19067629 |
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