Properties of soluble α-chymotrypsin in neat glycerol and water

Autores
Castro, Guillermo Raul
Año de publicación
2000
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
UV scanning of a-chymotrypsin dissolved in neat glycerol and water showed no significant differences in its spectra at pH 7.8. Fluorescence scanning revealed a strong dependence on pH values (between 5.9 to 10.5) of the maximum wavelength emission in water and no pH-dependence in 99% glycerol supplemented with 1% of appropriate buffers. The profile of a-chymotrypsin activity dissolved in water-glycerol mixtures with phenyl acetate as substrate displayed two maximum: highest peak was found at 100% water, and the second one was observed in 99% glycerol concentration with about 40% of the relative activity. Optimum pH of the soluble a-chymotrypsin in glycerol showed a displacement of 1 pH/U towards the alkaline side compared to water at pH 8.0. Kinetic and thermodynamic analysis using kinetic measurements of the thermal stability of a-chymotrypsin showed a higher inactivation rate in neat glycerol as compared to water in 30 to 45°C range, however, when temperature increases enzyme stability in glycerol is better than water. Thermostability of trypsin and a-chymotrypsin dissolved in glycerol at 100°C showed a half reaction time of approximately 7 and 20 h, respectively, and less than 1 minute in aqueous buffer for both enzymes.
Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Massachusetts Institute of Technology; Estados Unidos
Materia
Homogeneous Biocatalysis
Enzymes in Organic Media
Α-Chymotrypsin
Trypsin
Glycerol
Enzyme Thermostability
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:11336/41719
Acceder
id CONICETDig_0fbb0b5332aa4074a043a9116e32186a
oai_identifier_str oai:ri.conicet.gov.ar:11336/41719
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Properties of soluble α-chymotrypsin in neat glycerol and waterCastro, Guillermo RaulHomogeneous BiocatalysisEnzymes in Organic MediaΑ-ChymotrypsinTrypsinGlycerolEnzyme Thermostabilityhttps://purl.org/becyt/ford/2.5https://purl.org/becyt/ford/2https://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2UV scanning of a-chymotrypsin dissolved in neat glycerol and water showed no significant differences in its spectra at pH 7.8. Fluorescence scanning revealed a strong dependence on pH values (between 5.9 to 10.5) of the maximum wavelength emission in water and no pH-dependence in 99% glycerol supplemented with 1% of appropriate buffers. The profile of a-chymotrypsin activity dissolved in water-glycerol mixtures with phenyl acetate as substrate displayed two maximum: highest peak was found at 100% water, and the second one was observed in 99% glycerol concentration with about 40% of the relative activity. Optimum pH of the soluble a-chymotrypsin in glycerol showed a displacement of 1 pH/U towards the alkaline side compared to water at pH 8.0. Kinetic and thermodynamic analysis using kinetic measurements of the thermal stability of a-chymotrypsin showed a higher inactivation rate in neat glycerol as compared to water in 30 to 45°C range, however, when temperature increases enzyme stability in glycerol is better than water. Thermostability of trypsin and a-chymotrypsin dissolved in glycerol at 100°C showed a half reaction time of approximately 7 and 20 h, respectively, and less than 1 minute in aqueous buffer for both enzymes.Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Massachusetts Institute of Technology; Estados UnidosElsevier Science Inc2000-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/41719Castro, Guillermo Raul; Properties of soluble α-chymotrypsin in neat glycerol and water; Elsevier Science Inc; Enzyme and Microbial Technology; 27; 1-2; 12-2000; 143-1500141-0229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/S0141-0229(00)00197-6info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022900001976info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T10:00:38Zoai:ri.conicet.gov.ar:11336/41719instacron: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:34982025-11-12 10:00:39.209CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Properties of soluble α-chymotrypsin in neat glycerol and water
title Properties of soluble α-chymotrypsin in neat glycerol and water
spellingShingle Properties of soluble α-chymotrypsin in neat glycerol and water
Castro, Guillermo Raul
Homogeneous Biocatalysis
Enzymes in Organic Media
Α-Chymotrypsin
Trypsin
Glycerol
Enzyme Thermostability
title_short Properties of soluble α-chymotrypsin in neat glycerol and water
title_full Properties of soluble α-chymotrypsin in neat glycerol and water
title_fullStr Properties of soluble α-chymotrypsin in neat glycerol and water
title_full_unstemmed Properties of soluble α-chymotrypsin in neat glycerol and water
title_sort Properties of soluble α-chymotrypsin in neat glycerol and water
dc.creator.none.fl_str_mv Castro, Guillermo Raul
author Castro, Guillermo Raul
author_facet Castro, Guillermo Raul
author_role author
dc.subject.none.fl_str_mv Homogeneous Biocatalysis
Enzymes in Organic Media
Α-Chymotrypsin
Trypsin
Glycerol
Enzyme Thermostability
topic Homogeneous Biocatalysis
Enzymes in Organic Media
Α-Chymotrypsin
Trypsin
Glycerol
Enzyme Thermostability
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.5
https://purl.org/becyt/ford/2
https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv UV scanning of a-chymotrypsin dissolved in neat glycerol and water showed no significant differences in its spectra at pH 7.8. Fluorescence scanning revealed a strong dependence on pH values (between 5.9 to 10.5) of the maximum wavelength emission in water and no pH-dependence in 99% glycerol supplemented with 1% of appropriate buffers. The profile of a-chymotrypsin activity dissolved in water-glycerol mixtures with phenyl acetate as substrate displayed two maximum: highest peak was found at 100% water, and the second one was observed in 99% glycerol concentration with about 40% of the relative activity. Optimum pH of the soluble a-chymotrypsin in glycerol showed a displacement of 1 pH/U towards the alkaline side compared to water at pH 8.0. Kinetic and thermodynamic analysis using kinetic measurements of the thermal stability of a-chymotrypsin showed a higher inactivation rate in neat glycerol as compared to water in 30 to 45°C range, however, when temperature increases enzyme stability in glycerol is better than water. Thermostability of trypsin and a-chymotrypsin dissolved in glycerol at 100°C showed a half reaction time of approximately 7 and 20 h, respectively, and less than 1 minute in aqueous buffer for both enzymes.
Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina. Massachusetts Institute of Technology; Estados Unidos
description UV scanning of a-chymotrypsin dissolved in neat glycerol and water showed no significant differences in its spectra at pH 7.8. Fluorescence scanning revealed a strong dependence on pH values (between 5.9 to 10.5) of the maximum wavelength emission in water and no pH-dependence in 99% glycerol supplemented with 1% of appropriate buffers. The profile of a-chymotrypsin activity dissolved in water-glycerol mixtures with phenyl acetate as substrate displayed two maximum: highest peak was found at 100% water, and the second one was observed in 99% glycerol concentration with about 40% of the relative activity. Optimum pH of the soluble a-chymotrypsin in glycerol showed a displacement of 1 pH/U towards the alkaline side compared to water at pH 8.0. Kinetic and thermodynamic analysis using kinetic measurements of the thermal stability of a-chymotrypsin showed a higher inactivation rate in neat glycerol as compared to water in 30 to 45°C range, however, when temperature increases enzyme stability in glycerol is better than water. Thermostability of trypsin and a-chymotrypsin dissolved in glycerol at 100°C showed a half reaction time of approximately 7 and 20 h, respectively, and less than 1 minute in aqueous buffer for both enzymes.
publishDate 2000
dc.date.none.fl_str_mv 2000-12
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/11336/41719
Castro, Guillermo Raul; Properties of soluble α-chymotrypsin in neat glycerol and water; Elsevier Science Inc; Enzyme and Microbial Technology; 27; 1-2; 12-2000; 143-150
0141-0229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/41719
identifier_str_mv Castro, Guillermo Raul; Properties of soluble α-chymotrypsin in neat glycerol and water; Elsevier Science Inc; Enzyme and Microbial Technology; 27; 1-2; 12-2000; 143-150
0141-0229
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/S0141-0229(00)00197-6
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022900001976
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
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
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_ 1848598491072299008
score 12.976206

Publicaciones similares