INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)

This work presents a comparative study of the influence of the nature of the substrate and the immobilization and laccase enzyme activity and stability. The supports employed were: hydrotalcite-like particles mechanism onsediments) S.A. Medina-Moreno, S. Huerta-Ochoa, C.A. surface. Two immobilizatio...

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Autores: A. Castro, I. González, F. Tzompantzi, G. Viniegra-González
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2013
País:México
Institución:Universidad Autónoma Metropolitana
Repositorio:Redalyc-UAM
OAI Identifier:oai:redalyc.org:62030721005
Acceso en línea:https://www.redalyc.org/articulo.oa?id=62030721005
Access Level:acceso abierto
Palabra clave:Ingeniería
thiol
laccase
hydrotalcite
glassy carbon
immobilization
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spelling INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)A. CastroI. GonzálezF. TzompantziG. Viniegra-GonzálezIngenieríathiollaccasehydrotalciteglassy carbonimmobilizationThis work presents a comparative study of the influence of the nature of the substrate and the immobilization and laccase enzyme activity and stability. The supports employed were: hydrotalcite-like particles mechanism onsediments) S.A. Medina-Moreno, S. Huerta-Ochoa, C.A. surface. Two immobilization mechanisms were applied: one (ZnAl2 ), amorphous silica crystals, and glassy carbon Lucho-Constantino, L. Aguilera-Vázquez, A. Jiménez- physical, by adsorption, Gutiérrez-Rojaschemical, with two versions of covalent bonding. In the first, using silanes González y M. and the other and glutaraldehyde (GA), in the second, thiols were used as anchoring reagents. Hydrotalcite and silica supports 259 Crecimiento, sobrevivencia y adaptación the enzyme by X-ray diffraction analysis (XRD), while in the case were characterized before and after immobilizingde Bifidobacterium infantis a condiciones ácidas of glassy carbon supports electrochemical characterization was performed. The catalytic properties Km and Kcat /Km (Growth, survival and adaptation of Bifidobacterium infantis to acidic conditions) of every enzymatic system were evaluated in a complementary fashion, as well as the free enzyme. The kinetic L. Mayorga-Reyes, P. Bustamante-Camilo, A. Gutiérrez-Nava, E. Barranco-Florido y A. Azaola- characterizations were done using ABTS (ammonium 2,2’azino-bis-(3-ethylbenzothiazoline-6-sulfonate acid)), as a reagent typical of laccase in 0.1 M acetate buffer solution pH 3.7. Efficiency of the enzyme adsorbed on each Espinosa support it was demonstrated that optimization of immobilization is decisive in the catalysis. Greater efficiency was the method of ethanol fermentation by Saccharomyces cerevisiae in the 265 Statistical approach to observed in the system that employed glassy carbon with either immobilization mechanism and these results are analogous with the of Valfor® zeolite NaA presence free enzyme.Universidad Autónoma Metropolitana2013info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdf1665-2738https://www.redalyc.org/articulo.oa?id=62030721005Revista Mexicana de Ingeniería Química (México) Num.2 Vol.12reponame:Redalyc-UAMinstname:Universidad Autónoma Metropolitanainstacron:UAMenhttp://www.redalyc.org/revista.oa?id=620Revista Mexicana de Ingeniería Químicainfo:eu-repo/semantics/openAccessoai:redalyc.org:620307210052025-03-05T19:09:40Z
dc.title.none.fl_str_mv INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
title INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
spellingShingle INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
A. Castro
Ingeniería
thiol
laccase
hydrotalcite
glassy carbon
immobilization
title_short INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
title_full INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
title_fullStr INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
title_full_unstemmed INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
title_sort INFLUENCE OF THE TYPE OF SUPPORT AND IMMOBILIZATION ON THE ACTIVITY AND STABILITY OF LACCASE ENZYME (Trametes versicolor)
dc.creator.none.fl_str_mv A. Castro
I. González
F. Tzompantzi
G. Viniegra-González
author A. Castro
author_facet A. Castro
I. González
F. Tzompantzi
G. Viniegra-González
author_role author
author2 I. González
F. Tzompantzi
G. Viniegra-González
author2_role author
author
author
dc.subject.none.fl_str_mv Ingeniería
thiol
laccase
hydrotalcite
glassy carbon
immobilization
topic Ingeniería
thiol
laccase
hydrotalcite
glassy carbon
immobilization
description This work presents a comparative study of the influence of the nature of the substrate and the immobilization and laccase enzyme activity and stability. The supports employed were: hydrotalcite-like particles mechanism onsediments) S.A. Medina-Moreno, S. Huerta-Ochoa, C.A. surface. Two immobilization mechanisms were applied: one (ZnAl2 ), amorphous silica crystals, and glassy carbon Lucho-Constantino, L. Aguilera-Vázquez, A. Jiménez- physical, by adsorption, Gutiérrez-Rojaschemical, with two versions of covalent bonding. In the first, using silanes González y M. and the other and glutaraldehyde (GA), in the second, thiols were used as anchoring reagents. Hydrotalcite and silica supports 259 Crecimiento, sobrevivencia y adaptación the enzyme by X-ray diffraction analysis (XRD), while in the case were characterized before and after immobilizingde Bifidobacterium infantis a condiciones ácidas of glassy carbon supports electrochemical characterization was performed. The catalytic properties Km and Kcat /Km (Growth, survival and adaptation of Bifidobacterium infantis to acidic conditions) of every enzymatic system were evaluated in a complementary fashion, as well as the free enzyme. The kinetic L. Mayorga-Reyes, P. Bustamante-Camilo, A. Gutiérrez-Nava, E. Barranco-Florido y A. Azaola- characterizations were done using ABTS (ammonium 2,2’azino-bis-(3-ethylbenzothiazoline-6-sulfonate acid)), as a reagent typical of laccase in 0.1 M acetate buffer solution pH 3.7. Efficiency of the enzyme adsorbed on each Espinosa support it was demonstrated that optimization of immobilization is decisive in the catalysis. Greater efficiency was the method of ethanol fermentation by Saccharomyces cerevisiae in the 265 Statistical approach to observed in the system that employed glassy carbon with either immobilization mechanism and these results are analogous with the of Valfor® zeolite NaA presence free enzyme.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv 1665-2738
https://www.redalyc.org/articulo.oa?id=62030721005
identifier_str_mv 1665-2738
url https://www.redalyc.org/articulo.oa?id=62030721005
dc.language.none.fl_str_mv en
language_invalid_str_mv en
dc.relation.none.fl_str_mv http://www.redalyc.org/revista.oa?id=620
dc.rights.none.fl_str_mv Revista Mexicana de Ingeniería Química
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Revista Mexicana de Ingeniería Química
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidad Autónoma Metropolitana
publisher.none.fl_str_mv Universidad Autónoma Metropolitana
dc.source.none.fl_str_mv Revista Mexicana de Ingeniería Química (México) Num.2 Vol.12
reponame:Redalyc-UAM
instname:Universidad Autónoma Metropolitana
instacron:UAM
instname_str Universidad Autónoma Metropolitana
instacron_str UAM
institution UAM
reponame_str Redalyc-UAM
collection Redalyc-UAM
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 14.964248

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