Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation

Autores
Asaro, Antonela; Paggi, Roberto Alejandro; de Castro, Rosana Esther; Lopez Mañanes, Alejandra Antonia
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In spite of its inherent physiological importance, studies on the occurrence, characteristics, and modulation of amylase in euryhaline crabs are lacking. We investigated the occurrence of amylase forms and the effect of acclimation to different salinities on their number and made a partial purification and characterization of the major form present in the hepatopancreas of Neohelice granulata. Zymogram analysis revealed 5 amylase forms in crabs acclimated to 35 psu (seawater) and 37 psu, and an additional band at 10 psu, but with a major form (29 kDa) in all cases, which was partially purified and characterized. Amylolytic activity was maximal between 30 and 40 °C; maintained at high NaCl concentrations (up to 4 M); increased by 5 mM K+, Li+, Co2+, and Mg2+ (36%–45%); inhibited by Cu2+, Zn2+, Cd2+, Fe2+, and Mn2+ (92.4% and 23.7%); not affected by Ni2+ or Ba2+; and enhanced almost 100% by Ca2+. Amylase exhibited Michaelis–Menten kinetics (starch: Km = 1.24 mg mL–1; glycogen: Km = 16.19 mg mL–1). The potential physiological significance and relationship to habitat conditions of the extra form in low salinity and the biochemical characteristics of the partially purified amylolytic activity (halotolerant, differential sensitivity to ions, capability to hydrolyze starch and glycogen) are discussed.
Fil: Asaro, Antonela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencia Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
Fil: Paggi, Roberto Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: de Castro, Rosana Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencia Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
Materia
Amylolytic Activity
Digestive Tract
Environment
Euryhaline Crabs
Phenotypic Flexibility
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:11336/62667

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network_name_str CONICET Digital (CONICET)
spelling Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulationAsaro, AntonelaPaggi, Roberto Alejandrode Castro, Rosana EstherLopez Mañanes, Alejandra AntoniaAmylolytic ActivityDigestive TractEnvironmentEuryhaline CrabsPhenotypic Flexibilityhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In spite of its inherent physiological importance, studies on the occurrence, characteristics, and modulation of amylase in euryhaline crabs are lacking. We investigated the occurrence of amylase forms and the effect of acclimation to different salinities on their number and made a partial purification and characterization of the major form present in the hepatopancreas of Neohelice granulata. Zymogram analysis revealed 5 amylase forms in crabs acclimated to 35 psu (seawater) and 37 psu, and an additional band at 10 psu, but with a major form (29 kDa) in all cases, which was partially purified and characterized. Amylolytic activity was maximal between 30 and 40 °C; maintained at high NaCl concentrations (up to 4 M); increased by 5 mM K+, Li+, Co2+, and Mg2+ (36%–45%); inhibited by Cu2+, Zn2+, Cd2+, Fe2+, and Mn2+ (92.4% and 23.7%); not affected by Ni2+ or Ba2+; and enhanced almost 100% by Ca2+. Amylase exhibited Michaelis–Menten kinetics (starch: Km = 1.24 mg mL–1; glycogen: Km = 16.19 mg mL–1). The potential physiological significance and relationship to habitat conditions of the extra form in low salinity and the biochemical characteristics of the partially purified amylolytic activity (halotolerant, differential sensitivity to ions, capability to hydrolyze starch and glycogen) are discussed.Fil: Asaro, Antonela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencia Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; ArgentinaFil: Paggi, Roberto Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: de Castro, Rosana Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencia Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; ArgentinaTubitak Scientific & Technical Research Council Turkey2016-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/62667Asaro, Antonela; Paggi, Roberto Alejandro; de Castro, Rosana Esther; Lopez Mañanes, Alejandra Antonia; Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation; Tubitak Scientific & Technical Research Council Turkey; Turkish Journal Of Zoology; 41; 3; 10-2016; 443-4531300-0179CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3906/zoo-1601-10info:eu-repo/semantics/altIdentifier/url/http://journals.tubitak.gov.tr/zoology/issues/zoo-17-41-3/zoo-41-3-8-1601-10.pdfinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:11Zoai:ri.conicet.gov.ar:11336/62667instacron: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:34982025-09-03 09:59:11.904CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation
title Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation
spellingShingle Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation
Asaro, Antonela
Amylolytic Activity
Digestive Tract
Environment
Euryhaline Crabs
Phenotypic Flexibility
title_short Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation
title_full Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation
title_fullStr Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation
title_full_unstemmed Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation
title_sort Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation
dc.creator.none.fl_str_mv Asaro, Antonela
Paggi, Roberto Alejandro
de Castro, Rosana Esther
Lopez Mañanes, Alejandra Antonia
author Asaro, Antonela
author_facet Asaro, Antonela
Paggi, Roberto Alejandro
de Castro, Rosana Esther
Lopez Mañanes, Alejandra Antonia
author_role author
author2 Paggi, Roberto Alejandro
de Castro, Rosana Esther
Lopez Mañanes, Alejandra Antonia
author2_role author
author
author
dc.subject.none.fl_str_mv Amylolytic Activity
Digestive Tract
Environment
Euryhaline Crabs
Phenotypic Flexibility
topic Amylolytic Activity
Digestive Tract
Environment
Euryhaline Crabs
Phenotypic Flexibility
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In spite of its inherent physiological importance, studies on the occurrence, characteristics, and modulation of amylase in euryhaline crabs are lacking. We investigated the occurrence of amylase forms and the effect of acclimation to different salinities on their number and made a partial purification and characterization of the major form present in the hepatopancreas of Neohelice granulata. Zymogram analysis revealed 5 amylase forms in crabs acclimated to 35 psu (seawater) and 37 psu, and an additional band at 10 psu, but with a major form (29 kDa) in all cases, which was partially purified and characterized. Amylolytic activity was maximal between 30 and 40 °C; maintained at high NaCl concentrations (up to 4 M); increased by 5 mM K+, Li+, Co2+, and Mg2+ (36%–45%); inhibited by Cu2+, Zn2+, Cd2+, Fe2+, and Mn2+ (92.4% and 23.7%); not affected by Ni2+ or Ba2+; and enhanced almost 100% by Ca2+. Amylase exhibited Michaelis–Menten kinetics (starch: Km = 1.24 mg mL–1; glycogen: Km = 16.19 mg mL–1). The potential physiological significance and relationship to habitat conditions of the extra form in low salinity and the biochemical characteristics of the partially purified amylolytic activity (halotolerant, differential sensitivity to ions, capability to hydrolyze starch and glycogen) are discussed.
Fil: Asaro, Antonela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencia Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
Fil: Paggi, Roberto Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: de Castro, Rosana Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Lopez Mañanes, Alejandra Antonia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Universidad Nacional de Mar del Plata. Facultad de Ciencia Exactas y Naturales. Instituto de Investigaciones Marinas y Costeras; Argentina
description In spite of its inherent physiological importance, studies on the occurrence, characteristics, and modulation of amylase in euryhaline crabs are lacking. We investigated the occurrence of amylase forms and the effect of acclimation to different salinities on their number and made a partial purification and characterization of the major form present in the hepatopancreas of Neohelice granulata. Zymogram analysis revealed 5 amylase forms in crabs acclimated to 35 psu (seawater) and 37 psu, and an additional band at 10 psu, but with a major form (29 kDa) in all cases, which was partially purified and characterized. Amylolytic activity was maximal between 30 and 40 °C; maintained at high NaCl concentrations (up to 4 M); increased by 5 mM K+, Li+, Co2+, and Mg2+ (36%–45%); inhibited by Cu2+, Zn2+, Cd2+, Fe2+, and Mn2+ (92.4% and 23.7%); not affected by Ni2+ or Ba2+; and enhanced almost 100% by Ca2+. Amylase exhibited Michaelis–Menten kinetics (starch: Km = 1.24 mg mL–1; glycogen: Km = 16.19 mg mL–1). The potential physiological significance and relationship to habitat conditions of the extra form in low salinity and the biochemical characteristics of the partially purified amylolytic activity (halotolerant, differential sensitivity to ions, capability to hydrolyze starch and glycogen) are discussed.
publishDate 2016
dc.date.none.fl_str_mv 2016-10
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/11336/62667
Asaro, Antonela; Paggi, Roberto Alejandro; de Castro, Rosana Esther; Lopez Mañanes, Alejandra Antonia; Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation; Tubitak Scientific & Technical Research Council Turkey; Turkish Journal Of Zoology; 41; 3; 10-2016; 443-453
1300-0179
CONICET Digital
CONICET
url http://hdl.handle.net/11336/62667
identifier_str_mv Asaro, Antonela; Paggi, Roberto Alejandro; de Castro, Rosana Esther; Lopez Mañanes, Alejandra Antonia; Amylase in the hepatopancreas of a euryhaline burrowing crab: Characteristics and modulation; Tubitak Scientific & Technical Research Council Turkey; Turkish Journal Of Zoology; 41; 3; 10-2016; 443-453
1300-0179
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3906/zoo-1601-10
info:eu-repo/semantics/altIdentifier/url/http://journals.tubitak.gov.tr/zoology/issues/zoo-17-41-3/zoo-41-3-8-1601-10.pdf
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 Tubitak Scientific & Technical Research Council Turkey
publisher.none.fl_str_mv Tubitak Scientific & Technical Research Council Turkey
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
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