Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis

Globulin-P was partially hydrolyzed with papain under specific conditions to study the resulting structural modifications. Under mild hydrolytic conditions, globulin-P polymers were cleaved to render their unitary constituents (280 kDa molecules). Under stronger hydrolytic conditions these unitary m...

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Authors: Castellani, Oscar Francisco, Martinez, Estela Nora, Añon, Maria Cristina
Format: article
Status:Published version
Publication Date:2000
Country:Argentina
Institution:Consejo Nacional de Investigaciones Científicas y Técnicas
Repository:CONICET Digital (CONICET)
Language:English
OAI Identifier:oai:ri.conicet.gov.ar:11336/113475
Online Access:http://hdl.handle.net/11336/113475
Access Level:Open access
Keyword:Amaranth
Globulin
Papain
Protein structure
Proteolysis
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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network_name_str Argentina
repository_id_str
spelling Amaranth Globulin Structure Modifications Induced by Enzymatic ProteolysisCastellani, Oscar FranciscoMartinez, Estela NoraAñon, Maria CristinaAmaranthGlobulinPapainProtein structureProteolysishttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Globulin-P was partially hydrolyzed with papain under specific conditions to study the resulting structural modifications. Under mild hydrolytic conditions, globulin-P polymers were cleaved to render their unitary constituents (280 kDa molecules). Under stronger hydrolytic conditions these unitary molecules were 13% smaller than those from nonhydrolyzed globulin. Moreover, these molecules remained assembled even though they contained degraded polypeptides. The monomeric (M) subunit and the A chains were preferentially cleaved under mild and intermediate hydrolytic conditions, whereas B chains remained with the same size. These results suggest that the M and A polypeptides might be located at an exposed site of the molecules resembling the structure of the legumins. The M subunit may be participating in the stabilization of globulin-P polymers, on the basis that these two species disappeared under the same hydrolytic conditions. Similar events such as those described in this paper might be taking place on globulin-P during germination of amaranth grain.Fil: Castellani, Oscar Francisco. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Martinez, Estela Nora. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaAmerican Chemical Society2000-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/113475Castellani, Oscar Francisco; Martinez, Estela Nora; Añon, Maria Cristina; Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis; American Chemical Society; Journal of Agricultural and Food Chemistry; 48; 11; 11-2000; 5624-56290021-85611520-5118CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://tinyurl.com/y45r95czinfo:eu-repo/semantics/altIdentifier/doi/10.1021/jf000624oinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T14:06:06Zoai:ri.conicet.gov.ar:11336/113475instacron: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:34982024-05-08 14:06:06.758CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
title Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
spellingShingle Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
Castellani, Oscar Francisco
Amaranth
Globulin
Papain
Protein structure
Proteolysis
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
title_full Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
title_fullStr Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
title_full_unstemmed Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
title_sort Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis
dc.creator.none.fl_str_mv Castellani, Oscar Francisco
Martinez, Estela Nora
Añon, Maria Cristina
author Castellani, Oscar Francisco
author_facet Castellani, Oscar Francisco
Martinez, Estela Nora
Añon, Maria Cristina
author_role author
author2 Martinez, Estela Nora
Añon, Maria Cristina
author2_role author
author
dc.subject.none.fl_str_mv Amaranth
Globulin
Papain
Protein structure
Proteolysis
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic Amaranth
Globulin
Papain
Protein structure
Proteolysis
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description Globulin-P was partially hydrolyzed with papain under specific conditions to study the resulting structural modifications. Under mild hydrolytic conditions, globulin-P polymers were cleaved to render their unitary constituents (280 kDa molecules). Under stronger hydrolytic conditions these unitary molecules were 13% smaller than those from nonhydrolyzed globulin. Moreover, these molecules remained assembled even though they contained degraded polypeptides. The monomeric (M) subunit and the A chains were preferentially cleaved under mild and intermediate hydrolytic conditions, whereas B chains remained with the same size. These results suggest that the M and A polypeptides might be located at an exposed site of the molecules resembling the structure of the legumins. The M subunit may be participating in the stabilization of globulin-P polymers, on the basis that these two species disappeared under the same hydrolytic conditions. Similar events such as those described in this paper might be taking place on globulin-P during germination of amaranth grain.
publishDate 2000
dc.date.none.fl_str_mv 2000-11
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/11336/113475
Castellani, Oscar Francisco; Martinez, Estela Nora; Añon, Maria Cristina; Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis; American Chemical Society; Journal of Agricultural and Food Chemistry; 48; 11; 11-2000; 5624-5629
0021-8561
1520-5118
CONICET Digital
CONICET
url http://hdl.handle.net/11336/113475
identifier_str_mv Castellani, Oscar Francisco; Martinez, Estela Nora; Añon, Maria Cristina; Amaranth Globulin Structure Modifications Induced by Enzymatic Proteolysis; American Chemical Society; Journal of Agricultural and Food Chemistry; 48; 11; 11-2000; 5624-5629
0021-8561
1520-5118
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://tinyurl.com/y45r95cz
info:eu-repo/semantics/altIdentifier/doi/10.1021/jf000624o
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 American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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_ 1799195854463041536
score 15,812429

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