Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides

ABSTRACT: The objective of this study was to optimize the conditions of enzymatic hydrolysis (type of enzyme, pH, temperature (T), substrate (S) and enzyme concentration (E)) to increase content of soluble peptides (P), antioxidant activities and degree of hydrolysis DH (%), in hydrolysates. Also, t...

Full description

Autores:
Zapata Montoya, José Edgar
Sierra Lopera, Leidy Maritza
Tipo de recurso:
Article of investigation
Fecha de publicación:
2021
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/42253
Acceso en línea:
https://hdl.handle.net/10495/42253
Palabra clave:
Antioxidantes
Antioxidants
Péptidos Bioactivos Dietéticos
Bioactive Peptides, Dietary
Hidrólisis enzimática
Enzymatic hydrolysis
Tilapia
Alcalase
http://aims.fao.org/aos/agrovoc/c_27512
http://aims.fao.org/aos/agrovoc/c_32720
https://id.nlm.nih.gov/mesh/D000975
https://id.nlm.nih.gov/mesh/D000097482
Rights
openAccess
License
https://creativecommons.org/licenses/by-nc-nd/4.0/
id UDEA2_10adab547761f435626c988e536d73cc
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/42253
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
dc.title.spa.fl_str_mv Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides
title Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides
spellingShingle Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides
Antioxidantes
Antioxidants
Péptidos Bioactivos Dietéticos
Bioactive Peptides, Dietary
Hidrólisis enzimática
Enzymatic hydrolysis
Tilapia
Alcalase
http://aims.fao.org/aos/agrovoc/c_27512
http://aims.fao.org/aos/agrovoc/c_32720
https://id.nlm.nih.gov/mesh/D000975
https://id.nlm.nih.gov/mesh/D000097482
title_short Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides
title_full Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides
title_fullStr Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides
title_full_unstemmed Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides
title_sort Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides
dc.creator.fl_str_mv Zapata Montoya, José Edgar
Sierra Lopera, Leidy Maritza
dc.contributor.author.none.fl_str_mv Zapata Montoya, José Edgar
Sierra Lopera, Leidy Maritza
dc.contributor.researchgroup.spa.fl_str_mv Grupo de Nutrición y Tecnología de Alimentos
dc.subject.decs.none.fl_str_mv Antioxidantes
Antioxidants
Péptidos Bioactivos Dietéticos
Bioactive Peptides, Dietary
topic Antioxidantes
Antioxidants
Péptidos Bioactivos Dietéticos
Bioactive Peptides, Dietary
Hidrólisis enzimática
Enzymatic hydrolysis
Tilapia
Alcalase
http://aims.fao.org/aos/agrovoc/c_27512
http://aims.fao.org/aos/agrovoc/c_32720
https://id.nlm.nih.gov/mesh/D000975
https://id.nlm.nih.gov/mesh/D000097482
dc.subject.agrovoc.none.fl_str_mv Hidrólisis enzimática
Enzymatic hydrolysis
Tilapia
dc.subject.proposal.spa.fl_str_mv Alcalase
dc.subject.agrovocuri.none.fl_str_mv http://aims.fao.org/aos/agrovoc/c_27512
http://aims.fao.org/aos/agrovoc/c_32720
dc.subject.meshuri.none.fl_str_mv https://id.nlm.nih.gov/mesh/D000975
https://id.nlm.nih.gov/mesh/D000097482
description ABSTRACT: The objective of this study was to optimize the conditions of enzymatic hydrolysis (type of enzyme, pH, temperature (T), substrate (S) and enzyme concentration (E)) to increase content of soluble peptides (P), antioxidant activities and degree of hydrolysis DH (%), in hydrolysates. Also, the effect of scaling up from a 0.5 L to a 7.5 L reactor, was evaluated. Hydrolysis was carried out for 3 h in a 500 mL reactor, with Alcalase1 2.4 L and Flavourzyme1 500 L enzymes. A second experimental design was then developed with S and E as factors, where DH, P and antioxidant activity, were response variables. The Alcalase1 2.4 L was the most productive enzyme, with optimal S and E of 45 g/L and 4.4 g/L, respectively. Its hydrolysates showed antioxidant activities with IC50 of 0.76 g/L, 12 g/L and 8 g/L for ABTS, FRAP and ICA, respectively. The scale up didn’t showed negative effect on the hydrolysis.
publishDate 2021
dc.date.issued.none.fl_str_mv 2021
dc.date.accessioned.none.fl_str_mv 2024-09-18T19:56:16Z
dc.date.available.none.fl_str_mv 2024-09-18T19:56:16Z
dc.type.spa.fl_str_mv Artículo de investigación
dc.type.coar.spa.fl_str_mv http://purl.org/coar/resource_type/c_2df8fbb1
dc.type.redcol.spa.fl_str_mv https://purl.org/redcol/resource_type/ART
dc.type.coarversion.spa.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.driver.spa.fl_str_mv info:eu-repo/semantics/article
dc.type.version.spa.fl_str_mv info:eu-repo/semantics/publishedVersion
format http://purl.org/coar/resource_type/c_2df8fbb1
status_str publishedVersion
dc.identifier.citation.spa.fl_str_mv Sierra-Lopera LM, Zapata-Montoya JE. Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides. Biotechnol Rep (Amst). 2021 Apr 3;30:e00611. doi: 10.1016/j.btre.2021.e00611.
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10495/42253
dc.identifier.doi.none.fl_str_mv 10.1016/j.btre.2021.e00611
dc.identifier.eissn.none.fl_str_mv 2215-017X
identifier_str_mv Sierra-Lopera LM, Zapata-Montoya JE. Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides. Biotechnol Rep (Amst). 2021 Apr 3;30:e00611. doi: 10.1016/j.btre.2021.e00611.
10.1016/j.btre.2021.e00611
2215-017X
url https://hdl.handle.net/10495/42253
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.ispartofjournalabbrev.spa.fl_str_mv Biotechnol. Rep.
dc.relation.citationendpage.spa.fl_str_mv 10
dc.relation.citationstartpage.spa.fl_str_mv 1
dc.relation.citationvolume.spa.fl_str_mv 30
dc.relation.ispartofjournal.spa.fl_str_mv Biotechnology Reports
dc.rights.uri.spa.fl_str_mv https://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.uri.*.fl_str_mv http://creativecommons.org/licenses/by-nc-nd/2.5/co/
dc.rights.accessrights.spa.fl_str_mv info:eu-repo/semantics/openAccess
dc.rights.coar.spa.fl_str_mv http://purl.org/coar/access_right/c_abf2
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/4.0/
http://creativecommons.org/licenses/by-nc-nd/2.5/co/
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.extent.spa.fl_str_mv 10 páginas
dc.format.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Elsevier
dc.publisher.place.spa.fl_str_mv Ámsterdam, Países Bajos
institution Universidad de Antioquia
bitstream.url.fl_str_mv https://bibliotecadigital.udea.edu.co/bitstreams/07513c7d-bd1d-449c-9ec9-4fbd07ca5f8a/download
https://bibliotecadigital.udea.edu.co/bitstreams/30d75de8-7af4-464d-a2b1-718d0c01ba35/download
https://bibliotecadigital.udea.edu.co/bitstreams/3e8a781a-825e-41b0-b750-4aa5e851bcc3/download
https://bibliotecadigital.udea.edu.co/bitstreams/53a76cb2-227e-4da1-a419-eceee4c88628/download
https://bibliotecadigital.udea.edu.co/bitstreams/527b2ad1-a9b6-45dd-9a13-77229b6be862/download
bitstream.checksum.fl_str_mv 3257885b9c4ed03b9ab15ab3a1354757
b88b088d9957e670ce3b3fbe2eedbc13
8a4605be74aa9ea9d79846c1fba20a33
6ff34e87a225a07c5f97863d83f686d1
a598c97f0739e5c64721b326bff1b932
bitstream.checksumAlgorithm.fl_str_mv MD5
MD5
MD5
MD5
MD5
repository.name.fl_str_mv Repositorio Institucional de la Universidad de Antioquia
repository.mail.fl_str_mv aplicacionbibliotecadigitalbiblioteca@udea.edu.co
_version_ 1851052144015179776
spelling Zapata Montoya, José EdgarSierra Lopera, Leidy MaritzaGrupo de Nutrición y Tecnología de Alimentos2024-09-18T19:56:16Z2024-09-18T19:56:16Z2021Sierra-Lopera LM, Zapata-Montoya JE. Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptides. Biotechnol Rep (Amst). 2021 Apr 3;30:e00611. doi: 10.1016/j.btre.2021.e00611.https://hdl.handle.net/10495/4225310.1016/j.btre.2021.e006112215-017XABSTRACT: The objective of this study was to optimize the conditions of enzymatic hydrolysis (type of enzyme, pH, temperature (T), substrate (S) and enzyme concentration (E)) to increase content of soluble peptides (P), antioxidant activities and degree of hydrolysis DH (%), in hydrolysates. Also, the effect of scaling up from a 0.5 L to a 7.5 L reactor, was evaluated. Hydrolysis was carried out for 3 h in a 500 mL reactor, with Alcalase1 2.4 L and Flavourzyme1 500 L enzymes. A second experimental design was then developed with S and E as factors, where DH, P and antioxidant activity, were response variables. The Alcalase1 2.4 L was the most productive enzyme, with optimal S and E of 45 g/L and 4.4 g/L, respectively. Its hydrolysates showed antioxidant activities with IC50 of 0.76 g/L, 12 g/L and 8 g/L for ABTS, FRAP and ICA, respectively. The scale up didn’t showed negative effect on the hydrolysis.Sistema General de Regalías de ColombiaUniversidad de Antioquia. Vicerrectoría de investigación. Comité para el Desarrollo de la Investigación - CODICOL001077110 páginasapplication/pdfengElsevierÁmsterdam, Países Bajoshttps://creativecommons.org/licenses/by-nc-nd/4.0/http://creativecommons.org/licenses/by-nc-nd/2.5/co/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Optimization of enzymatic hydrolysis of red tilapia scales (Oreochromis sp.) to obtain bioactive peptidesArtículo de investigaciónhttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARThttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionAntioxidantesAntioxidantsPéptidos Bioactivos DietéticosBioactive Peptides, DietaryHidrólisis enzimáticaEnzymatic hydrolysisTilapiaAlcalasehttp://aims.fao.org/aos/agrovoc/c_27512http://aims.fao.org/aos/agrovoc/c_32720https://id.nlm.nih.gov/mesh/D000975https://id.nlm.nih.gov/mesh/D000097482Biotechnol. Rep.10130Biotechnology ReportsRoR:05x7bg352RoR:03bp5hc83PublicationORIGINALZapataJosé_2021_Optimization_Enzymatic_Hydrolysis.pdfZapataJosé_2021_Optimization_Enzymatic_Hydrolysis.pdfArtículo de investigaciónapplication/pdf1072628https://bibliotecadigital.udea.edu.co/bitstreams/07513c7d-bd1d-449c-9ec9-4fbd07ca5f8a/download3257885b9c4ed03b9ab15ab3a1354757MD51trueAnonymousREADCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8823https://bibliotecadigital.udea.edu.co/bitstreams/30d75de8-7af4-464d-a2b1-718d0c01ba35/downloadb88b088d9957e670ce3b3fbe2eedbc13MD52falseAnonymousREADLICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://bibliotecadigital.udea.edu.co/bitstreams/3e8a781a-825e-41b0-b750-4aa5e851bcc3/download8a4605be74aa9ea9d79846c1fba20a33MD53falseAnonymousREADTEXTZapataJosé_2021_Optimization_Enzymatic_Hydrolysis.pdf.txtZapataJosé_2021_Optimization_Enzymatic_Hydrolysis.pdf.txtExtracted texttext/plain66539https://bibliotecadigital.udea.edu.co/bitstreams/53a76cb2-227e-4da1-a419-eceee4c88628/download6ff34e87a225a07c5f97863d83f686d1MD56falseAnonymousREADTHUMBNAILZapataJosé_2021_Optimization_Enzymatic_Hydrolysis.pdf.jpgZapataJosé_2021_Optimization_Enzymatic_Hydrolysis.pdf.jpgGenerated Thumbnailimage/jpeg16410https://bibliotecadigital.udea.edu.co/bitstreams/527b2ad1-a9b6-45dd-9a13-77229b6be862/downloada598c97f0739e5c64721b326bff1b932MD57falseAnonymousREAD10495/42253oai:bibliotecadigital.udea.edu.co:10495/422532025-03-26 17:38:35.273https://creativecommons.org/licenses/by-nc-nd/4.0/open.accesshttps://bibliotecadigital.udea.edu.coRepositorio Institucional de la Universidad de Antioquiaaplicacionbibliotecadigitalbiblioteca@udea.edu.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