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...

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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
Atribución-NoComercial-SinDerivadas 2.5 Colombia
id UDEA2_f8d3c2ac8a305ade9a83bd4f7cbdb45f
oai_identifier_str oai:bibliotecadigital.udea.edu.co:10495/11714
network_acronym_str UDEA2
network_name_str Repositorio UdeA
repository_id_str
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.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 info:eu-repo/semantics/article
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
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dc.type.redcol.spa.fl_str_mv https://purl.org/redcol/resource_type/ART
dc.type.local.spa.fl_str_mv Artículo de investigación
format http://purl.org/coar/resource_type/c_2df8fbb1
status_str publishedVersion
dc.identifier.citation.spa.fl_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
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.rights.*.fl_str_mv Atribución-NoComercial-SinDerivadas 2.5 Colombia
dc.rights.spa.fl_str_mv info:eu-repo/semantics/openAccess
dc.rights.uri.*.fl_str_mv http://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 Colombia
http://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.mimetype.spa.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv MDPI AG
dc.publisher.group.spa.fl_str_mv Alimentación y Nutrición Humana
Impacto de Componentes Alimentarios en la Salud
dc.publisher.place.spa.fl_str_mv Suiza
institution Universidad de Antioquia
bitstream.url.fl_str_mv http://bibliotecadigital.udea.edu.co/bitstream/10495/11714/2/license.txt
http://bibliotecadigital.udea.edu.co/bitstream/10495/11714/1/JulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdf
bitstream.checksum.fl_str_mv 8a4605be74aa9ea9d79846c1fba20a33
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repository.name.fl_str_mv Repositorio Institucional Universidad de Antioquia
repository.mail.fl_str_mv andres.perez@udea.edu.co
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spelling Bassan, Juliana Cristinade Souza Bezerra, Thaís MilenaPeixoto, GuilhermePaulino da Cruz, Clariana ZanuttoMartínez Galán, Julián Pauldos Santos Vaz, Aline BudaSantesso Garrido, SauloFilice, MarcoMonti, Rubens2019-08-22T18:29:37Z2019-08-22T18:29:37Z2016Bassan 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 AGAlimentación y Nutrición HumanaImpacto de Componentes Alimentarios en la SaludSuizainfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARTArtículo de investigaciónhttp://purl.org/coar/version/c_970fb48d4fbd8a85Atribución-NoComercial-SinDerivadas 2.5 Colombiainfo:eu-repo/semantics/openAccesshttp://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/Corn cob powder functionalizedTrypsinImmobilizationReactorWhey protein hydrolysatesPeptidesImmobilization of trypsin in lignocellulosic waste material to produce peptides with bioactive potential from whey proteinMaterialsMaterials12095LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/11714/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52ORIGINALJulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdfJulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdfArtículo de investigaciónapplication/pdf6993538http://bibliotecadigital.udea.edu.co/bitstream/10495/11714/1/JulianaBassan_2016_ImmobilizationTrypsinLignocellulosicWaste.pdff0ea4dbddc9fafeaafc78b853faf2ec1MD5110495/11714oai:bibliotecadigital.udea.edu.co:10495/117142021-10-25 13:39:02.963Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.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