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...
- 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
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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 |
dc.type.coarversion.fl_str_mv |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
dc.type.hasversion.spa.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.coar.spa.fl_str_mv |
http://purl.org/coar/resource_type/c_3248 |
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 |
dc.rights.uri.*.fl_str_mv |
https://creativecommons.org/licenses/by-nc-nd/2.5/co/ |
dc.rights.accessrights.spa.fl_str_mv |
http://purl.org/coar/access_right/c_abf2 |
dc.rights.creativecommons.spa.fl_str_mv |
https://creativecommons.org/licenses/by-nc-nd/4.0/ |
rights_invalid_str_mv |
Atribución-NoComercial-SinDerivadas 2.5 https://creativecommons.org/licenses/by-nc-nd/2.5/co/ http://purl.org/coar/access_right/c_abf2 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 http://bibliotecadigital.udea.edu.co/bitstream/10495/17075/2/license_rdf |
bitstream.checksum.fl_str_mv |
8a4605be74aa9ea9d79846c1fba20a33 73017b6167a9ce1f17bef7231ad3a19b 1646d1f6b96dbbbc38035efc9239ac9c |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositorio Institucional Universidad de Antioquia |
repository.mail.fl_str_mv |
andres.perez@udea.edu.co |
_version_ |
1812173223835467776 |
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.coTk9URTogUExBQ0UgWU9VUiBPV04gTElDRU5TRSBIRVJFClRoaXMgc2FtcGxlIGxpY2Vuc2UgaXMgcHJvdmlkZWQgZm9yIGluZm9ybWF0aW9uYWwgcHVycG9zZXMgb25seS4KCk5PTi1FWENMVVNJVkUgRElTVFJJQlVUSU9OIExJQ0VOU0UKCkJ5IHNpZ25pbmcgYW5kIHN1Ym1pdHRpbmcgdGhpcyBsaWNlbnNlLCB5b3UgKHRoZSBhdXRob3Iocykgb3IgY29weXJpZ2h0Cm93bmVyKSBncmFudHMgdG8gRFNwYWNlIFVuaXZlcnNpdHkgKERTVSkgdGhlIG5vbi1leGNsdXNpdmUgcmlnaHQgdG8gcmVwcm9kdWNlLAp0cmFuc2xhdGUgKGFzIGRlZmluZWQgYmVsb3cpLCBhbmQvb3IgZGlzdHJpYnV0ZSB5b3VyIHN1Ym1pc3Npb24gKGluY2x1ZGluZwp0aGUgYWJzdHJhY3QpIHdvcmxkd2lkZSBpbiBwcmludCBhbmQgZWxlY3Ryb25pYyBmb3JtYXQgYW5kIGluIGFueSBtZWRpdW0sCmluY2x1ZGluZyBidXQgbm90IGxpbWl0ZWQgdG8gYXVkaW8gb3IgdmlkZW8uCgpZb3UgYWdyZWUgdGhhdCBEU1UgbWF5LCB3aXRob3V0IGNoYW5naW5nIHRoZSBjb250ZW50LCB0cmFuc2xhdGUgdGhlCnN1Ym1pc3Npb24gdG8gYW55IG1lZGl1bSBvciBmb3JtYXQgZm9yIHRoZSBwdXJwb3NlIG9mIHByZXNlcnZhdGlvbi4KCllvdSBhbHNvIGFncmVlIHRoYXQgRFNVIG1heSBrZWVwIG1vcmUgdGhhbiBvbmUgY29weSBvZiB0aGlzIHN1Ym1pc3Npb24gZm9yCnB1cnBvc2VzIG9mIHNlY3VyaXR5LCBiYWNrLXVwIGFuZCBwcmVzZXJ2YXRpb24uCgpZb3UgcmVwcmVzZW50IHRoYXQgdGhlIHN1Ym1pc3Npb24gaXMgeW91ciBvcmlnaW5hbCB3b3JrLCBhbmQgdGhhdCB5b3UgaGF2ZQp0aGUgcmlnaHQgdG8gZ3JhbnQgdGhlIHJpZ2h0cyBjb250YWluZWQgaW4gdGhpcyBsaWNlbnNlLiBZb3UgYWxzbyByZXByZXNlbnQKdGhhdCB5b3VyIHN1Ym1pc3Npb24gZG9lcyBub3QsIHRvIHRoZSBiZXN0IG9mIHlvdXIga25vd2xlZGdlLCBpbmZyaW5nZSB1cG9uCmFueW9uZSdzIGNvcHlyaWdodC4KCklmIHRoZSBzdWJtaXNzaW9uIGNvbnRhaW5zIG1hdGVyaWFsIGZvciB3aGljaCB5b3UgZG8gbm90IGhvbGQgY29weXJpZ2h0LAp5b3UgcmVwcmVzZW50IHRoYXQgeW91IGhhdmUgb2J0YWluZWQgdGhlIHVucmVzdHJpY3RlZCBwZXJtaXNzaW9uIG9mIHRoZQpjb3B5cmlnaHQgb3duZXIgdG8gZ3JhbnQgRFNVIHRoZSByaWdodHMgcmVxdWlyZWQgYnkgdGhpcyBsaWNlbnNlLCBhbmQgdGhhdApzdWNoIHRoaXJkLXBhcnR5IG93bmVkIG1hdGVyaWFsIGlzIGNsZWFybHkgaWRlbnRpZmllZCBhbmQgYWNrbm93bGVkZ2VkCndpdGhpbiB0aGUgdGV4dCBvciBjb250ZW50IG9mIHRoZSBzdWJtaXNzaW9uLgoKSUYgVEhFIFNVQk1JU1NJT04gSVMgQkFTRUQgVVBPTiBXT1JLIFRIQVQgSEFTIEJFRU4gU1BPTlNPUkVEIE9SIFNVUFBPUlRFRApCWSBBTiBBR0VOQ1kgT1IgT1JHQU5JWkFUSU9OIE9USEVSIFRIQU4gRFNVLCBZT1UgUkVQUkVTRU5UIFRIQVQgWU9VIEhBVkUKRlVMRklMTEVEIEFOWSBSSUdIVCBPRiBSRVZJRVcgT1IgT1RIRVIgT0JMSUdBVElPTlMgUkVRVUlSRUQgQlkgU1VDSApDT05UUkFDVCBPUiBBR1JFRU1FTlQuCgpEU1Ugd2lsbCBjbGVhcmx5IGlkZW50aWZ5IHlvdXIgbmFtZShzKSBhcyB0aGUgYXV0aG9yKHMpIG9yIG93bmVyKHMpIG9mIHRoZQpzdWJtaXNzaW9uLCBhbmQgd2lsbCBub3QgbWFrZSBhbnkgYWx0ZXJhdGlvbiwgb3RoZXIgdGhhbiBhcyBhbGxvd2VkIGJ5IHRoaXMKbGljZW5zZSwgdG8geW91ciBzdWJtaXNzaW9uLgo= |