Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds

ABSTRACT: Plant-derived proteins are remarkable macromolecules of scientific interest because they represent an alternative to the animal-derived proteins and petroleum-derived polymers. Many food proteins especially those derived from animal sources could act as antigens in humans. For instance, mi...

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Autores:
Quintero Quiroz, Julián
Naranjo Durán, Ana María
Ciro Gómez, Gelmy Luz
Rojas Camargo, John Jairo
Tipo de recurso:
Part of book
Fecha de publicación:
2017
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/17075
Acceso en línea:
http://hdl.handle.net/10495/17075
Palabra clave:
Aminoácidos, Péptidos y Proteínas
Amino Acids, Peptides, and Proteins
Proteínas vegetales
Plant proteins
Compuestos bioactivos
Bioactive compounds
Encapsulación
Encapsulation
Rights
openAccess
License
Atribución-NoComercial-SinDerivadas 2.5
id UDEA2_7fa446318257ec942b151e6fa95a48b3
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/17075
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds
title Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds
spellingShingle Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds
Aminoácidos, Péptidos y Proteínas
Amino Acids, Peptides, and Proteins
Proteínas vegetales
Plant proteins
Compuestos bioactivos
Bioactive compounds
Encapsulación
Encapsulation
title_short Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds
title_full Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds
title_fullStr Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds
title_full_unstemmed Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds
title_sort Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive Compounds
dc.creator.fl_str_mv Quintero Quiroz, Julián
Naranjo Durán, Ana María
Ciro Gómez, Gelmy Luz
Rojas Camargo, John Jairo
dc.contributor.author.none.fl_str_mv Quintero Quiroz, Julián
Naranjo Durán, Ana María
Ciro Gómez, Gelmy Luz
Rojas Camargo, John Jairo
dc.subject.decs.none.fl_str_mv Aminoácidos, Péptidos y Proteínas
Amino Acids, Peptides, and Proteins
topic Aminoácidos, Péptidos y Proteínas
Amino Acids, Peptides, and Proteins
Proteínas vegetales
Plant proteins
Compuestos bioactivos
Bioactive compounds
Encapsulación
Encapsulation
dc.subject.lemb.none.fl_str_mv Proteínas vegetales
Plant proteins
Compuestos bioactivos
Bioactive compounds
dc.subject.proposal.spa.fl_str_mv Encapsulación
Encapsulation
description ABSTRACT: Plant-derived proteins are remarkable macromolecules of scientific interest because they represent an alternative to the animal-derived proteins and petroleum-derived polymers. Many food proteins especially those derived from animal sources could act as antigens in humans. For instance, milk proteins extracted from cows may cause food intolerance during infancy. Further, soybean, peanuts, tree nuts, fish, crustacean shellfish and egg proteins may act as antigens in 90% of children. Since the GI tract is permeable to intact antigens the oral intake of these proteins may generate gastrointestinal (50–80%), cutaneous (20-40%) and respiratory symptoms (4–25%). Most of these allergens are water-soluble glycoproteins that are resistant to acids and enzymes. Usually, these proteins have a small molecular weight (10,000–60,000 kDa), water solubility, glycosylation residues, and a relative resistance to heat and digestion. Allergenicity is less frequent in vegetable proteins due to their less flexible and non-compact structure. Allergenicity is also related to the resistance to proteolysis, post-translational glycosylation, presence of epitopes, and enzymatic proteolysis. Moreover, proteins serve as a coating material if structural modifications in the protein, either by physical, chemical or enzymatic mechanisms are conducted. As a result, their allergenicity is reduced, and their functional properties are enhanced.
publishDate 2017
dc.date.issued.none.fl_str_mv 2017
dc.date.accessioned.none.fl_str_mv 2020-10-26T16:10:09Z
dc.date.available.none.fl_str_mv 2020-10-26T16:10:09Z
dc.type.spa.fl_str_mv info:eu-repo/semantics/bookPart
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dc.type.redcol.spa.fl_str_mv https://purl.org/redcol/resource_type/CAP_LIB
dc.type.local.spa.fl_str_mv Capítulo de libro
format http://purl.org/coar/resource_type/c_3248
status_str publishedVersion
dc.identifier.isbn.none.fl_str_mv 978-953-51-3568-5
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/10495/17075
dc.identifier.doi.none.fl_str_mv 10.5772/intechopen.70378
identifier_str_mv 978-953-51-3568-5
10.5772/intechopen.70378
url http://hdl.handle.net/10495/17075
dc.language.iso.spa.fl_str_mv eng
language eng
dc.rights.*.fl_str_mv Atribución-NoComercial-SinDerivadas 2.5
dc.rights.spa.fl_str_mv info:eu-repo/semantics/openAccess
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rights_invalid_str_mv Atribución-NoComercial-SinDerivadas 2.5
https://creativecommons.org/licenses/by-nc-nd/2.5/co/
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https://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.extent.spa.fl_str_mv 25
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv intechopen
institution Universidad de Antioquia
bitstream.url.fl_str_mv http://bibliotecadigital.udea.edu.co/bitstream/10495/17075/3/license.txt
http://bibliotecadigital.udea.edu.co/bitstream/10495/17075/1/QuinteroJulian_2017_VegetableProteindCompounds.pdf
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repository.name.fl_str_mv Repositorio Institucional Universidad de Antioquia
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spelling Quintero Quiroz, JuliánNaranjo Durán, Ana MaríaCiro Gómez, Gelmy LuzRojas Camargo, John Jairo2020-10-26T16:10:09Z2020-10-26T16:10:09Z2017978-953-51-3568-5http://hdl.handle.net/10495/1707510.5772/intechopen.70378ABSTRACT: Plant-derived proteins are remarkable macromolecules of scientific interest because they represent an alternative to the animal-derived proteins and petroleum-derived polymers. Many food proteins especially those derived from animal sources could act as antigens in humans. For instance, milk proteins extracted from cows may cause food intolerance during infancy. Further, soybean, peanuts, tree nuts, fish, crustacean shellfish and egg proteins may act as antigens in 90% of children. Since the GI tract is permeable to intact antigens the oral intake of these proteins may generate gastrointestinal (50–80%), cutaneous (20-40%) and respiratory symptoms (4–25%). Most of these allergens are water-soluble glycoproteins that are resistant to acids and enzymes. Usually, these proteins have a small molecular weight (10,000–60,000 kDa), water solubility, glycosylation residues, and a relative resistance to heat and digestion. Allergenicity is less frequent in vegetable proteins due to their less flexible and non-compact structure. Allergenicity is also related to the resistance to proteolysis, post-translational glycosylation, presence of epitopes, and enzymatic proteolysis. Moreover, proteins serve as a coating material if structural modifications in the protein, either by physical, chemical or enzymatic mechanisms are conducted. As a result, their allergenicity is reduced, and their functional properties are enhanced.25application/pdfengintechopeninfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/bookParthttp://purl.org/coar/resource_type/c_3248https://purl.org/redcol/resource_type/CAP_LIBCapítulo de librohttp://purl.org/coar/version/c_970fb48d4fbd8a85Atribución-NoComercial-SinDerivadas 2.5info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/co/http://purl.org/coar/access_right/c_abf2https://creativecommons.org/licenses/by-nc-nd/4.0/Vegetable Proteins : Non-sensitizing Encapsulation Agents for Bioactive CompoundsAminoácidos, Péptidos y ProteínasAmino Acids, Peptides, and ProteinsProteínas vegetalesPlant proteinsCompuestos bioactivosBioactive compoundsEncapsulaciónEncapsulationAllergen4365LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/17075/3/license.txt8a4605be74aa9ea9d79846c1fba20a33MD53ORIGINALQuinteroJulian_2017_VegetableProteindCompounds.pdfQuinteroJulian_2017_VegetableProteindCompounds.pdfCapítulo de libroapplication/pdf2864160http://bibliotecadigital.udea.edu.co/bitstream/10495/17075/1/QuinteroJulian_2017_VegetableProteindCompounds.pdf73017b6167a9ce1f17bef7231ad3a19bMD51CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8927http://bibliotecadigital.udea.edu.co/bitstream/10495/17075/2/license_rdf1646d1f6b96dbbbc38035efc9239ac9cMD5210495/17075oai:bibliotecadigital.udea.edu.co:10495/170752021-03-24 14:11:23.478Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.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