Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties

Trabajo presentado en el VII Workshop on Biocatalysis and Biotransformations - 1º Simposio Latinoamericano de Biocatalisis y Biotransformaciones, celebrado en Búzios (Brasil) del 23 al 26 de septiembre de 2014. [Introduction]: Chemical modification of enzymes is a strategy widely used in biocatalysi...

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Main Authors: Barbosa, Oveimar, Rueda, Nazzoly, Torres Sáez, Rodrigo, Ortiz, Claudia, Fernández-Lafuente, Roberto
Other Authors: Universidad Industrial de Santander (Colombia), Ministerio de Ciencia e Innovación (España), Colciencias (Colombia)
Format: Still Image
Language:unknown
Published: 2014
Subjects:
Uis
Online Access:http://hdl.handle.net/10261/189392
https://doi.org/10.13039/501100004837
https://doi.org/10.13039/501100009087
id ftcsic:oai:digital.csic.es:10261/189392
record_format openpolar
spelling ftcsic:oai:digital.csic.es:10261/189392 2024-02-11T09:57:11+01:00 Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties Barbosa, Oveimar Rueda, Nazzoly Torres Sáez, Rodrigo Ortiz, Claudia Fernández-Lafuente, Roberto Universidad Industrial de Santander (Colombia) Ministerio de Ciencia e Innovación (España) Colciencias (Colombia) 2014-09-23 http://hdl.handle.net/10261/189392 https://doi.org/10.13039/501100004837 https://doi.org/10.13039/501100009087 unknown #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2013- 41507-R Publisher's version Sí VII Workshop on Biocatalysis and Biotransformations - 1º Simposio Latinoamericano de Biocatalisis y Biotransformaciones (2014) http://hdl.handle.net/10261/189392 http://dx.doi.org/10.13039/501100004837 http://dx.doi.org/10.13039/501100009087 open Immobilization Solid-phase chemical modification Enzyme hyperactivation póster de congreso http://purl.org/coar/resource_type/c_6670 2014 ftcsic https://doi.org/10.13039/50110000483710.13039/501100009087 2024-01-16T10:43:02Z Trabajo presentado en el VII Workshop on Biocatalysis and Biotransformations - 1º Simposio Latinoamericano de Biocatalisis y Biotransformaciones, celebrado en Búzios (Brasil) del 23 al 26 de septiembre de 2014. [Introduction]: Chemical modification of enzymes is a strategy widely used in biocatalysis for design of biocatalysts with improved biochemical properties. when the chemical modification is performed on immobilized enzymes, we can protect the enzyme from side-effects that are normally produced with modification of the soluble form of the enzymes. In this work, we modified CALB through two differentmethodologies, and the effect of these modification on the activity, stability and specificity of the enzyme was studied. [Results and discussion]: The effect of chemical modification on the enzyme activity of CALB immobilized on octyl-agarose (OC) and Cyanogen Bromide-agarose (BrCN) were evaluated. In Table 1 are shown changes in enzyme activity of CALB by chemical modification produced by modification (100%) with EDA and TNBS.In Table 2 are shown enzyme activity and enantioselectivity of the different derivatives on (R/S)-Methyl mandelate. Modification of lipase caused different activity and enatioselectivity results, demonstrating that both activity and selectivity of lipase are affected depending on the type of enzyme modification. [Conclusion]: This work exemplifies as chemical modification on solid phase allows modulating biochemical properties of lipases, affecting activity, stability and enantioselectivity of these enzymes. This work was funded by COLCIENCIAS (Project No. 1102-489-25428), Universidad Industrial de Santander (VIE-UIS) and by Ministerio de Ciencia e Innovación from Spain (CTQ2013- 41507-R ). Peer Reviewed Still Image Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Uis ENVELOPE(141.975,141.975,60.184,60.184)
institution Open Polar
collection Digital.CSIC (Spanish National Research Council)
op_collection_id ftcsic
language unknown
topic Immobilization
Solid-phase chemical modification
Enzyme hyperactivation
spellingShingle Immobilization
Solid-phase chemical modification
Enzyme hyperactivation
Barbosa, Oveimar
Rueda, Nazzoly
Torres Sáez, Rodrigo
Ortiz, Claudia
Fernández-Lafuente, Roberto
Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties
topic_facet Immobilization
Solid-phase chemical modification
Enzyme hyperactivation
description Trabajo presentado en el VII Workshop on Biocatalysis and Biotransformations - 1º Simposio Latinoamericano de Biocatalisis y Biotransformaciones, celebrado en Búzios (Brasil) del 23 al 26 de septiembre de 2014. [Introduction]: Chemical modification of enzymes is a strategy widely used in biocatalysis for design of biocatalysts with improved biochemical properties. when the chemical modification is performed on immobilized enzymes, we can protect the enzyme from side-effects that are normally produced with modification of the soluble form of the enzymes. In this work, we modified CALB through two differentmethodologies, and the effect of these modification on the activity, stability and specificity of the enzyme was studied. [Results and discussion]: The effect of chemical modification on the enzyme activity of CALB immobilized on octyl-agarose (OC) and Cyanogen Bromide-agarose (BrCN) were evaluated. In Table 1 are shown changes in enzyme activity of CALB by chemical modification produced by modification (100%) with EDA and TNBS.In Table 2 are shown enzyme activity and enantioselectivity of the different derivatives on (R/S)-Methyl mandelate. Modification of lipase caused different activity and enatioselectivity results, demonstrating that both activity and selectivity of lipase are affected depending on the type of enzyme modification. [Conclusion]: This work exemplifies as chemical modification on solid phase allows modulating biochemical properties of lipases, affecting activity, stability and enantioselectivity of these enzymes. This work was funded by COLCIENCIAS (Project No. 1102-489-25428), Universidad Industrial de Santander (VIE-UIS) and by Ministerio de Ciencia e Innovación from Spain (CTQ2013- 41507-R ). Peer Reviewed
author2 Universidad Industrial de Santander (Colombia)
Ministerio de Ciencia e Innovación (España)
Colciencias (Colombia)
format Still Image
author Barbosa, Oveimar
Rueda, Nazzoly
Torres Sáez, Rodrigo
Ortiz, Claudia
Fernández-Lafuente, Roberto
author_facet Barbosa, Oveimar
Rueda, Nazzoly
Torres Sáez, Rodrigo
Ortiz, Claudia
Fernández-Lafuente, Roberto
author_sort Barbosa, Oveimar
title Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties
title_short Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties
title_full Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties
title_fullStr Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties
title_full_unstemmed Chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties
title_sort chemical modification of lipase b of candida antarctica in solid phase for improving biochemical properties
publishDate 2014
url http://hdl.handle.net/10261/189392
https://doi.org/10.13039/501100004837
https://doi.org/10.13039/501100009087
long_lat ENVELOPE(141.975,141.975,60.184,60.184)
geographic Uis
geographic_facet Uis
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2013- 41507-R
Publisher's version

VII Workshop on Biocatalysis and Biotransformations - 1º Simposio Latinoamericano de Biocatalisis y Biotransformaciones (2014)
http://hdl.handle.net/10261/189392
http://dx.doi.org/10.13039/501100004837
http://dx.doi.org/10.13039/501100009087
op_rights open
op_doi https://doi.org/10.13039/50110000483710.13039/501100009087
_version_ 1790609402170966016