Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein
ABSTRACT: In this study, trypsin (Enzyme Comission 3.4.21.4) was immobilized in a low cost, lignocellulosic support (corn cob powder—CCP) with the goal of obtaining peptides with bioactive potential from cheese whey. The pretreated support was activated with glyoxyl groups, glutaraldehyde and IDA-gl...
- Autores:
-
Bassan, Juliana Cristina
de Souza Bezerra, Thaís Milena
Peixoto, Guilherme
Paulino da Cruz, Clariana Zanutto
Martínez Galán, Julián Paul
dos Santos Vaz, Aline Buda
Santesso Garrido, Saulo
Filice, Marco
Monti, Rubens
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2016
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/11714
- Acceso en línea:
- http://hdl.handle.net/10495/11714
- Palabra clave:
- Corn cob powder functionalized
Trypsin
Immobilization
Reactor
Whey protein hydrolysates
Peptides
- Rights
- openAccess
- License
- https://creativecommons.org/licenses/by-nc-nd/4.0/
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| dc.title.spa.fl_str_mv |
Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein |
| title |
Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein |
| spellingShingle |
Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein Corn cob powder functionalized Trypsin Immobilization Reactor Whey protein hydrolysates Peptides |
| title_short |
Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein |
| title_full |
Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein |
| title_fullStr |
Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein |
| title_full_unstemmed |
Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein |
| title_sort |
Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein |
| dc.creator.fl_str_mv |
Bassan, Juliana Cristina de Souza Bezerra, Thaís Milena Peixoto, Guilherme Paulino da Cruz, Clariana Zanutto Martínez Galán, Julián Paul dos Santos Vaz, Aline Buda Santesso Garrido, Saulo Filice, Marco Monti, Rubens |
| dc.contributor.author.none.fl_str_mv |
Bassan, Juliana Cristina de Souza Bezerra, Thaís Milena Peixoto, Guilherme Paulino da Cruz, Clariana Zanutto Martínez Galán, Julián Paul dos Santos Vaz, Aline Buda Santesso Garrido, Saulo Filice, Marco Monti, Rubens |
| dc.contributor.researchgroup.spa.fl_str_mv |
Alimentación y Nutrición Humana Impacto de Componentes Alimentarios en la Salud |
| dc.subject.none.fl_str_mv |
Corn cob powder functionalized Trypsin Immobilization Reactor Whey protein hydrolysates Peptides |
| topic |
Corn cob powder functionalized Trypsin Immobilization Reactor Whey protein hydrolysates Peptides |
| description |
ABSTRACT: In this study, trypsin (Enzyme Comission 3.4.21.4) was immobilized in a low cost, lignocellulosic support (corn cob powder—CCP) with the goal of obtaining peptides with bioactive potential from cheese whey. The pretreated support was activated with glyoxyl groups, glutaraldehyde and IDA-glyoxyl. The immobilization yields of the derivatives were higher than 83%, and the retention of catalytic activity was higher than 74%. The trypsin-glyoxyl-CCP derivative was thermally stable at 65 ̋C, a value that was 1090-fold higher than that obtained with the free enzyme. The trypsin-IDA-glyoxyl-CCP and trypsin-glutaraldehyde-CCP derivatives had thermal stabilities that were 883- and five-fold higher, respectively, then those obtained with the free enzyme. In the batch experiments, trypsin-IDA-glyoxyl-CCP retained 91% of its activity and had a degree of hydrolysis of 12.49%, while the values for trypsin-glyoxyl-CCP were 87% and 15.46%, respectively. The stabilized derivative trypsin-glyoxyl-CCP was also tested in an upflow packed-bed reactor. The hydrodynamic characterization of this reactor was a plug flow pattern, and the kinetics of this system provided a relative activity of 3.04 ̆ 0.01 U ̈ g ́1 and an average degree of hydrolysis of 23%, which were suitable for the production of potentially bioactive peptides. |
| publishDate |
2016 |
| dc.date.issued.none.fl_str_mv |
2016 |
| dc.date.accessioned.none.fl_str_mv |
2019-08-22T18:29:37Z |
| dc.date.available.none.fl_str_mv |
2019-08-22T18:29:37Z |
| dc.type.spa.fl_str_mv |
Artículo de investigación |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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https://purl.org/redcol/resource_type/ART |
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http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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info:eu-repo/semantics/article |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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Bassan J, de Souza-Bezerra T, Peixoto G, Paulino-da-Cruz C, Martínez-Galán J, et al. Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein. Materials. 2016; 9(5), 357. DOI: 10.3390/ma9050357 |
| dc.identifier.issn.none.fl_str_mv |
1996-1944 |
| dc.identifier.uri.none.fl_str_mv |
http://hdl.handle.net/10495/11714 |
| identifier_str_mv |
Bassan J, de Souza-Bezerra T, Peixoto G, Paulino-da-Cruz C, Martínez-Galán J, et al. Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein. Materials. 2016; 9(5), 357. DOI: 10.3390/ma9050357 1996-1944 |
| url |
http://hdl.handle.net/10495/11714 |
| dc.language.iso.spa.fl_str_mv |
eng |
| language |
eng |
| dc.relation.ispartofjournalabbrev.spa.fl_str_mv |
Materials |
| dc.relation.citationendpage.spa.fl_str_mv |
20 |
| dc.relation.citationissue.spa.fl_str_mv |
5 |
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1 |
| dc.relation.citationvolume.spa.fl_str_mv |
9 |
| dc.relation.ispartofjournal.spa.fl_str_mv |
Materials |
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https://creativecommons.org/licenses/by-nc-nd/4.0/ |
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http://creativecommons.org/licenses/by-nc-nd/2.5/co/ |
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Atribución-NoComercial-SinDerivadas 2.5 Colombia |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
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MDPI AG |
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Suiza |
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Universidad de Antioquia |
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Bassan, Juliana Cristinade Souza Bezerra, Thaís MilenaPeixoto, GuilhermePaulino da Cruz, Clariana ZanuttoMartínez Galán, Julián Pauldos Santos Vaz, Aline BudaSantesso Garrido, SauloFilice, MarcoMonti, RubensAlimentación y Nutrición HumanaImpacto de Componentes Alimentarios en la Salud2019-08-22T18:29:37Z2019-08-22T18:29:37Z2016Bassan J, de Souza-Bezerra T, Peixoto G, Paulino-da-Cruz C, Martínez-Galán J, et al. Immobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey protein. Materials. 2016; 9(5), 357. DOI: 10.3390/ma90503571996-1944http://hdl.handle.net/10495/11714ABSTRACT: In this study, trypsin (Enzyme Comission 3.4.21.4) was immobilized in a low cost, lignocellulosic support (corn cob powder—CCP) with the goal of obtaining peptides with bioactive potential from cheese whey. The pretreated support was activated with glyoxyl groups, glutaraldehyde and IDA-glyoxyl. The immobilization yields of the derivatives were higher than 83%, and the retention of catalytic activity was higher than 74%. The trypsin-glyoxyl-CCP derivative was thermally stable at 65 ̋C, a value that was 1090-fold higher than that obtained with the free enzyme. The trypsin-IDA-glyoxyl-CCP and trypsin-glutaraldehyde-CCP derivatives had thermal stabilities that were 883- and five-fold higher, respectively, then those obtained with the free enzyme. In the batch experiments, trypsin-IDA-glyoxyl-CCP retained 91% of its activity and had a degree of hydrolysis of 12.49%, while the values for trypsin-glyoxyl-CCP were 87% and 15.46%, respectively. The stabilized derivative trypsin-glyoxyl-CCP was also tested in an upflow packed-bed reactor. The hydrodynamic characterization of this reactor was a plug flow pattern, and the kinetics of this system provided a relative activity of 3.04 ̆ 0.01 U ̈ g ́1 and an average degree of hydrolysis of 23%, which were suitable for the production of potentially bioactive peptides.application/pdfengMDPI AGSuizahttps://creativecommons.org/licenses/by-nc-nd/4.0/http://creativecommons.org/licenses/by-nc-nd/2.5/co/Atribución-NoComercial-SinDerivadas 2.5 Colombiainfo:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Corn cob powder functionalizedTrypsinImmobilizationReactorWhey protein hydrolysatesPeptidesImmobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey proteinArtículo 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/publishedVersionMaterials20519MaterialsPublicationLICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://bibliotecadigital.udea.edu.co/bitstreams/b6b12986-d359-4d2d-8fd2-25ff373e6e21/download8a4605be74aa9ea9d79846c1fba20a33MD52falseAnonymousREADORIGINALJulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdfJulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdfArtículo de investigaciónapplication/pdf6993538https://bibliotecadigital.udea.edu.co/bitstreams/1e6c7dfa-b4be-43b1-a756-cfdfe5449c73/downloadf0ea4dbddc9fafeaafc78b853faf2ec1MD51trueAnonymousREADTEXTJulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdf.txtJulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdf.txtExtracted texttext/plain85413https://bibliotecadigital.udea.edu.co/bitstreams/6ab7de73-68ea-4b25-a059-a9f8935da68f/download9abc2e08723ebddb3e52a9993580bb3bMD53falseAnonymousREADTHUMBNAILJulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdf.jpgJulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdf.jpgGenerated Thumbnailimage/jpeg14641https://bibliotecadigital.udea.edu.co/bitstreams/1387f485-f7c3-43b4-b2ba-4cfdac72c41f/download32d8f31cebc99900750434c399b4a99fMD54falseAnonymousREAD10495/11714oai:bibliotecadigital.udea.edu.co:10495/117142025-03-26 20:48:09.458https://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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 |