Membrane topology modulates β-galactosidase activity against soluble substrates

Autores
Sanchez, Julieta Maria; Perillo, Maria Angelica
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The effect of bio-surfaces of contrasting curvature, on the kinetic parameters of ortho-nitrophenyl-β-D-galactopiranoside hydrolysis catalyzed by E. coli β-galactosidase, was investigated. The self-aggregating state and structure of the amphiphiles (Phosphatidylcholine, Lubrol-PX, Triton X-100, DocNa, SDS and CTAB) were inferred from their c.m.c. values and light-scattering measurements. Low curvature phosphatidylcholine or mixed phosphatidylcholine-detergent vesicles increased V max without affecting K M. High curvature micellar structures containing ionic detergents modulated negatively the enzyme activity (decreased or abolished V max and increased K M). Neither micelles containing non-ionic detergents nor the amphiphiles in a monomeric form, affected enzyme activity. CTAB at a concentration bellow its c.m.c but incorporated into a bilayer, became an activator (K M decreased respect to the control). Non-enzymatic interfacial hydrolysis of the substrate was discarded. Enzyme-membrane interaction and membrane elasticity, were evaluated using monomolecular layers at the air-water interface. Beyond particular molecular structures, topology affected the direction of the modulatory effects exerted by these amphiphiles on β-galactosidase activity. © 2002 Elsevier Science B.V. All rights reserved.
Fil: Sanchez, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Materia
Β-Galactosidase Activity
Enzyme-Surface Interaction
Micelles
Monomolecular Layers
Surface Curvature
Vesicles
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/64525
Acceder
id CONICETDig_00b760ca34dd260a4fff4c46de9e95f2
oai_identifier_str oai:ri.conicet.gov.ar:11336/64525
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Membrane topology modulates β-galactosidase activity against soluble substratesSanchez, Julieta MariaPerillo, Maria AngelicaΒ-Galactosidase ActivityEnzyme-Surface InteractionMicellesMonomolecular LayersSurface CurvatureVesicleshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The effect of bio-surfaces of contrasting curvature, on the kinetic parameters of ortho-nitrophenyl-β-D-galactopiranoside hydrolysis catalyzed by E. coli β-galactosidase, was investigated. The self-aggregating state and structure of the amphiphiles (Phosphatidylcholine, Lubrol-PX, Triton X-100, DocNa, SDS and CTAB) were inferred from their c.m.c. values and light-scattering measurements. Low curvature phosphatidylcholine or mixed phosphatidylcholine-detergent vesicles increased V max without affecting K M. High curvature micellar structures containing ionic detergents modulated negatively the enzyme activity (decreased or abolished V max and increased K M). Neither micelles containing non-ionic detergents nor the amphiphiles in a monomeric form, affected enzyme activity. CTAB at a concentration bellow its c.m.c but incorporated into a bilayer, became an activator (K M decreased respect to the control). Non-enzymatic interfacial hydrolysis of the substrate was discarded. Enzyme-membrane interaction and membrane elasticity, were evaluated using monomolecular layers at the air-water interface. Beyond particular molecular structures, topology affected the direction of the modulatory effects exerted by these amphiphiles on β-galactosidase activity. © 2002 Elsevier Science B.V. All rights reserved.Fil: Sanchez, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaFil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaElsevier Science2002-11-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/64525Sanchez, Julieta Maria; Perillo, Maria Angelica; Membrane topology modulates β-galactosidase activity against soluble substrates; Elsevier Science; Biophysical Chemistry; 99; 3; 6-11-2002; 281-2950301-4622CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0301462202002296info:eu-repo/semantics/altIdentifier/doi/10.1016/S0301-4622(02)00229-6info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:36:00Zoai:ri.conicet.gov.ar:11336/64525instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:36:00.746CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Membrane topology modulates β-galactosidase activity against soluble substrates
title Membrane topology modulates β-galactosidase activity against soluble substrates
spellingShingle Membrane topology modulates β-galactosidase activity against soluble substrates
Sanchez, Julieta Maria
Β-Galactosidase Activity
Enzyme-Surface Interaction
Micelles
Monomolecular Layers
Surface Curvature
Vesicles
title_short Membrane topology modulates β-galactosidase activity against soluble substrates
title_full Membrane topology modulates β-galactosidase activity against soluble substrates
title_fullStr Membrane topology modulates β-galactosidase activity against soluble substrates
title_full_unstemmed Membrane topology modulates β-galactosidase activity against soluble substrates
title_sort Membrane topology modulates β-galactosidase activity against soluble substrates
dc.creator.none.fl_str_mv Sanchez, Julieta Maria
Perillo, Maria Angelica
author Sanchez, Julieta Maria
author_facet Sanchez, Julieta Maria
Perillo, Maria Angelica
author_role author
author2 Perillo, Maria Angelica
author2_role author
dc.subject.none.fl_str_mv Β-Galactosidase Activity
Enzyme-Surface Interaction
Micelles
Monomolecular Layers
Surface Curvature
Vesicles
topic Β-Galactosidase Activity
Enzyme-Surface Interaction
Micelles
Monomolecular Layers
Surface Curvature
Vesicles
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The effect of bio-surfaces of contrasting curvature, on the kinetic parameters of ortho-nitrophenyl-β-D-galactopiranoside hydrolysis catalyzed by E. coli β-galactosidase, was investigated. The self-aggregating state and structure of the amphiphiles (Phosphatidylcholine, Lubrol-PX, Triton X-100, DocNa, SDS and CTAB) were inferred from their c.m.c. values and light-scattering measurements. Low curvature phosphatidylcholine or mixed phosphatidylcholine-detergent vesicles increased V max without affecting K M. High curvature micellar structures containing ionic detergents modulated negatively the enzyme activity (decreased or abolished V max and increased K M). Neither micelles containing non-ionic detergents nor the amphiphiles in a monomeric form, affected enzyme activity. CTAB at a concentration bellow its c.m.c but incorporated into a bilayer, became an activator (K M decreased respect to the control). Non-enzymatic interfacial hydrolysis of the substrate was discarded. Enzyme-membrane interaction and membrane elasticity, were evaluated using monomolecular layers at the air-water interface. Beyond particular molecular structures, topology affected the direction of the modulatory effects exerted by these amphiphiles on β-galactosidase activity. © 2002 Elsevier Science B.V. All rights reserved.
Fil: Sanchez, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
description The effect of bio-surfaces of contrasting curvature, on the kinetic parameters of ortho-nitrophenyl-β-D-galactopiranoside hydrolysis catalyzed by E. coli β-galactosidase, was investigated. The self-aggregating state and structure of the amphiphiles (Phosphatidylcholine, Lubrol-PX, Triton X-100, DocNa, SDS and CTAB) were inferred from their c.m.c. values and light-scattering measurements. Low curvature phosphatidylcholine or mixed phosphatidylcholine-detergent vesicles increased V max without affecting K M. High curvature micellar structures containing ionic detergents modulated negatively the enzyme activity (decreased or abolished V max and increased K M). Neither micelles containing non-ionic detergents nor the amphiphiles in a monomeric form, affected enzyme activity. CTAB at a concentration bellow its c.m.c but incorporated into a bilayer, became an activator (K M decreased respect to the control). Non-enzymatic interfacial hydrolysis of the substrate was discarded. Enzyme-membrane interaction and membrane elasticity, were evaluated using monomolecular layers at the air-water interface. Beyond particular molecular structures, topology affected the direction of the modulatory effects exerted by these amphiphiles on β-galactosidase activity. © 2002 Elsevier Science B.V. All rights reserved.
publishDate 2002
dc.date.none.fl_str_mv 2002-11-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/64525
Sanchez, Julieta Maria; Perillo, Maria Angelica; Membrane topology modulates β-galactosidase activity against soluble substrates; Elsevier Science; Biophysical Chemistry; 99; 3; 6-11-2002; 281-295
0301-4622
CONICET Digital
CONICET
url http://hdl.handle.net/11336/64525
identifier_str_mv Sanchez, Julieta Maria; Perillo, Maria Angelica; Membrane topology modulates β-galactosidase activity against soluble substrates; Elsevier Science; Biophysical Chemistry; 99; 3; 6-11-2002; 281-295
0301-4622
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0301462202002296
info:eu-repo/semantics/altIdentifier/doi/10.1016/S0301-4622(02)00229-6
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844614379482382336
score 13.070432

Publicaciones similares