Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments

ABSTRACT: Proteins are macromolecules exhibiting amphiphilic properties, good biocompatibility, biodegradability, high nutritional value, and show strong interactions with several types of active compounds via hydrogen bonding and electrostatic interactions (1). These plant or animal-derived macromo...

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Autores:
Quintero Quiroz, Julián
Rojas Camargo, John Jairo
Tipo de recurso:
Editorial
Fecha de publicación:
2018
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
spa
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/17076
Acceso en línea:
http://hdl.handle.net/10495/17076
Palabra clave:
Proteínas vegetales
Plant proteins
Editorial
Macromoleculas
Macromolecules
Rights
openAccess
License
Atribución-NoComercial-CompartirIgual 2.5 Colombia (CC BY-NC-SA 2.5 CO)
id UDEA2_fb01cc57f2a4a6a2cc8fc6d042c5b742
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/17076
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments
title Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments
spellingShingle Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments
Proteínas vegetales
Plant proteins
Editorial
Macromoleculas
Macromolecules
title_short Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments
title_full Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments
title_fullStr Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments
title_full_unstemmed Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments
title_sort Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments
dc.creator.fl_str_mv Quintero Quiroz, Julián
Rojas Camargo, John Jairo
dc.contributor.author.none.fl_str_mv Quintero Quiroz, Julián
Rojas Camargo, John Jairo
dc.subject.decs.none.fl_str_mv Proteínas vegetales
Plant proteins
Editorial
topic Proteínas vegetales
Plant proteins
Editorial
Macromoleculas
Macromolecules
dc.subject.lemb.none.fl_str_mv Macromoleculas
Macromolecules
description ABSTRACT: Proteins are macromolecules exhibiting amphiphilic properties, good biocompatibility, biodegradability, high nutritional value, and show strong interactions with several types of active compounds via hydrogen bonding and electrostatic interactions (1). These plant or animal-derived macromolecules differ in their molecular size depending on the number of amino acids present in their structure, which in turn, are linked by peptide bonds between the carbonyl (-CO-) and amino groups (-NH) (2). This amino acid sequence has its particular three-dimensional or folded organization, which provides each protein with (i) technofunctional characteristics (i.e., gelling, emulsifying, coagulating and encapsulating capabilities, softener, adsorbents, etc); (ii) biological (i.e., nutritional value, transport, and other enzymatic functions); and (iii) bioactive (i.e., antioxidant, antimicrobial, anticoagulant or anti-inflammatory activities) characteristics, which are essential in the pharmaceutical and food fields (3). Another factor that affects the functional characteristics of proteins is their source. Thus, proteins derived from vegetable sources are larger, less flexible, and less soluble in extreme pH ranges. Further, they have a globular conformation with more hydrophobic groups hidden within the molecular structure as compared to the animal counterparts (4). However, animal-derived proteins are the most widely used due to their easy processing and water solubility. In order to match those characteristics vegetable proteins can be functionalized, making them more biodegradable and biocompatible. Moreover, they are renewable, highly available, their productions implies less natural resources, and are considered as “environmentally economical”
publishDate 2018
dc.date.issued.none.fl_str_mv 2018
dc.date.accessioned.none.fl_str_mv 2020-10-26T16:35:23Z
dc.date.available.none.fl_str_mv 2020-10-26T16:35:23Z
dc.type.spa.fl_str_mv info:eu-repo/semantics/contributionToPeriodical
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dc.type.coar.spa.fl_str_mv http://purl.org/coar/resource_type/c_b239
dc.type.redcol.spa.fl_str_mv https://purl.org/redcol/resource_type/ARTEDIT
dc.type.local.spa.fl_str_mv Editorial
format http://purl.org/coar/resource_type/c_b239
status_str publishedVersion
dc.identifier.issn.none.fl_str_mv 0121-4004
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/10495/17076
dc.identifier.doi.none.fl_str_mv 10.17533/udea.vitae.v25n1a01
dc.identifier.eissn.none.fl_str_mv 2145-2660
identifier_str_mv 0121-4004
10.17533/udea.vitae.v25n1a01
2145-2660
url http://hdl.handle.net/10495/17076
dc.language.iso.spa.fl_str_mv spa
language spa
dc.relation.ispartofjournalabbrev.spa.fl_str_mv Vitae
dc.rights.*.fl_str_mv Atribución-NoComercial-CompartirIgual 2.5 Colombia (CC BY-NC-SA 2.5 CO)
dc.rights.spa.fl_str_mv info:eu-repo/semantics/openAccess
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rights_invalid_str_mv Atribución-NoComercial-CompartirIgual 2.5 Colombia (CC BY-NC-SA 2.5 CO)
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eu_rights_str_mv openAccess
dc.format.extent.spa.fl_str_mv 2
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Universidad de Antioquia, Facultad de Ciencias Farmacéuticas y Alimentarias
dc.publisher.place.spa.fl_str_mv Medellín, Colombia
institution Universidad de Antioquia
bitstream.url.fl_str_mv http://bibliotecadigital.udea.edu.co/bitstream/10495/17076/1/QuinteroJulian_2018_ProteinsStrategyMacromolecules.pdf
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spelling Quintero Quiroz, JuliánRojas Camargo, John Jairo2020-10-26T16:35:23Z2020-10-26T16:35:23Z20180121-4004http://hdl.handle.net/10495/1707610.17533/udea.vitae.v25n1a012145-2660ABSTRACT: Proteins are macromolecules exhibiting amphiphilic properties, good biocompatibility, biodegradability, high nutritional value, and show strong interactions with several types of active compounds via hydrogen bonding and electrostatic interactions (1). These plant or animal-derived macromolecules differ in their molecular size depending on the number of amino acids present in their structure, which in turn, are linked by peptide bonds between the carbonyl (-CO-) and amino groups (-NH) (2). This amino acid sequence has its particular three-dimensional or folded organization, which provides each protein with (i) technofunctional characteristics (i.e., gelling, emulsifying, coagulating and encapsulating capabilities, softener, adsorbents, etc); (ii) biological (i.e., nutritional value, transport, and other enzymatic functions); and (iii) bioactive (i.e., antioxidant, antimicrobial, anticoagulant or anti-inflammatory activities) characteristics, which are essential in the pharmaceutical and food fields (3). Another factor that affects the functional characteristics of proteins is their source. Thus, proteins derived from vegetable sources are larger, less flexible, and less soluble in extreme pH ranges. Further, they have a globular conformation with more hydrophobic groups hidden within the molecular structure as compared to the animal counterparts (4). However, animal-derived proteins are the most widely used due to their easy processing and water solubility. In order to match those characteristics vegetable proteins can be functionalized, making them more biodegradable and biocompatible. Moreover, they are renewable, highly available, their productions implies less natural resources, and are considered as “environmentally economical”2application/pdfspaUniversidad de Antioquia, Facultad de Ciencias Farmacéuticas y AlimentariasMedellín, Colombiainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/contributionToPeriodicalhttp://purl.org/coar/resource_type/c_b239http://purl.org/coar/resource_type/c_3e5ahttps://purl.org/redcol/resource_type/ARTEDITEditorialhttp://purl.org/coar/version/c_970fb48d4fbd8a85Atribución-NoComercial-CompartirIgual 2.5 Colombia (CC BY-NC-SA 2.5 CO)info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/co/http://purl.org/coar/access_right/c_abf2https://creativecommons.org/licenses/by-nc-sa/4.0/Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food DevelopmentsProteínas vegetalesPlant proteinsEditorialMacromoleculasMacromoleculesVitaeVitae67251ORIGINALQuinteroJulian_2018_ProteinsStrategyMacromolecules.pdfQuinteroJulian_2018_ProteinsStrategyMacromolecules.pdfEditorialapplication/pdf138931http://bibliotecadigital.udea.edu.co/bitstream/10495/17076/1/QuinteroJulian_2018_ProteinsStrategyMacromolecules.pdfa13d009019038bec3cec2093548f8be8MD51CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-81045http://bibliotecadigital.udea.edu.co/bitstream/10495/17076/2/license_rdf21f304c81bfa79d3db42c7e2740dd6feMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/17076/3/license.txt8a4605be74aa9ea9d79846c1fba20a33MD5310495/17076oai:bibliotecadigital.udea.edu.co:10495/170762021-03-24 13:41:16.875Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.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