Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero
ABSTRACT: The whey is the largest waste subproduct of the dairy industry. Due to its high values of BOD is considered a source of water and soil contamination when discarded without any treatment. An alternative for the disposal of this agroindustrial waste is its application as a culture medium for...
- Autores:
-
Beltrán Flórez, Laura Julliet
Acosta Cárdenas, Alejandro
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2012
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- spa
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/10193
- Acceso en línea:
- http://hdl.handle.net/10495/10193
- Palabra clave:
- Beta-Galactosidasa
Galactosidasa
Hidrólisis enzimática
Kluyveromyces
Lactosuero
Suero de leche
Enzymatic hydrolysis
Whey
- Rights
- openAccess
- License
- Atribución-NoComercial-CompartirIgual 2.5 Colombia (CC BY-NC-SA 2.5 CO)
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dc.title.spa.fl_str_mv |
Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero |
dc.title.alternative.spa.fl_str_mv |
Usage of a commercial β-galactosidase from Kluyveromyces lactis in the hydrolysis of whey |
title |
Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero |
spellingShingle |
Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero Beta-Galactosidasa Galactosidasa Hidrólisis enzimática Kluyveromyces Lactosuero Suero de leche Enzymatic hydrolysis Whey |
title_short |
Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero |
title_full |
Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero |
title_fullStr |
Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero |
title_full_unstemmed |
Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero |
title_sort |
Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero |
dc.creator.fl_str_mv |
Beltrán Flórez, Laura Julliet Acosta Cárdenas, Alejandro |
dc.contributor.author.none.fl_str_mv |
Beltrán Flórez, Laura Julliet Acosta Cárdenas, Alejandro |
dc.subject.none.fl_str_mv |
Beta-Galactosidasa Galactosidasa Hidrólisis enzimática Kluyveromyces Lactosuero Suero de leche Enzymatic hydrolysis Whey |
topic |
Beta-Galactosidasa Galactosidasa Hidrólisis enzimática Kluyveromyces Lactosuero Suero de leche Enzymatic hydrolysis Whey |
description |
ABSTRACT: The whey is the largest waste subproduct of the dairy industry. Due to its high values of BOD is considered a source of water and soil contamination when discarded without any treatment. An alternative for the disposal of this agroindustrial waste is its application as a culture medium for various fermentation processes after an enzymatic hydrolysis thus ensuring a greater availability of fermentable sugars for subsequent application in biotechnology, environment and / or food. Objective To evaluate the effects of pH, temperature and enzyme concentration on whey using a commercial β-galactosidase from Kluyveromyces lactis, and determine the kinetic parameters of the enzyme. Materials and methods The hydrolysis of lactose was performed in buffered solutions of lactose and in whey as well, 5 levels were evaluated for pH (4.5-8.5), temperature (25°C-65°C) and enzyme concentration (0.025 g/L to 0.5 g/L), all the experiments were performed in triplicate in Erlenmeyer flask (100 mL) and analyzed using the GraphPad Prism software. Results We found that the best conditions of pH and temperature for the whey hydrolysis were at 6,5°C and 45°C respectively. According to the kinetic results, the enzyme presented competitive inhibition for galactose with a Km equal to 8.01x10-2 M, Ki of 6.85x10-2 M and Vmax of 1.86x10-2 molmg-1min-1. Conclusions The best conditions of pH and temperature were 6.5°C and 45°C respectively, a 100% of hydrolysis was achieved in one hour with 0.1 g/L of enzyme. Furthermore, it was shown that the reaction rate of the enzyme is inhibited by galactose. |
publishDate |
2012 |
dc.date.issued.none.fl_str_mv |
2012 |
dc.date.accessioned.none.fl_str_mv |
2018-10-04T21:49:57Z |
dc.date.available.none.fl_str_mv |
2018-10-04T21:49:57Z |
dc.type.spa.fl_str_mv |
info:eu-repo/semantics/article |
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_2df8fbb1 |
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 |
Beltrán Flórez, LJ, Acosta Cárdenas, A. . Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero. Hechos Microbiol. 2012; 3(2);25-35. |
dc.identifier.issn.none.fl_str_mv |
2145-8898 |
dc.identifier.uri.none.fl_str_mv |
http://hdl.handle.net/10495/10193 |
dc.identifier.eissn.none.fl_str_mv |
2805-6485 |
identifier_str_mv |
Beltrán Flórez, LJ, Acosta Cárdenas, A. . Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero. Hechos Microbiol. 2012; 3(2);25-35. 2145-8898 2805-6485 |
url |
http://hdl.handle.net/10495/10193 |
dc.language.iso.spa.fl_str_mv |
spa |
language |
spa |
dc.relation.ispartofjournalabbrev.spa.fl_str_mv |
Hechos Microbiol. |
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 |
dc.rights.uri.*.fl_str_mv |
https://creativecommons.org/licenses/by-nc-sa/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-sa/4.0/ |
rights_invalid_str_mv |
Atribución-NoComercial-CompartirIgual 2.5 Colombia (CC BY-NC-SA 2.5 CO) https://creativecommons.org/licenses/by-nc-sa/2.5/co/ http://purl.org/coar/access_right/c_abf2 https://creativecommons.org/licenses/by-nc-sa/4.0/ |
eu_rights_str_mv |
openAccess |
dc.format.mimetype.spa.fl_str_mv |
application/pdf |
dc.publisher.spa.fl_str_mv |
Universidad de Antioquia, Escuela de Microbiología |
dc.publisher.group.spa.fl_str_mv |
Grupo de Biotransformación |
dc.publisher.place.spa.fl_str_mv |
Medellín, Colombia |
institution |
Universidad de Antioquia |
bitstream.url.fl_str_mv |
http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/1/BeltranLaura_2012_GalactosidasacomercialHidrolisis.pdf http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/2/license_url http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/3/license_text http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/4/license_rdf http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/5/license.txt |
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spelling |
Beltrán Flórez, Laura JullietAcosta Cárdenas, Alejandro2018-10-04T21:49:57Z2018-10-04T21:49:57Z2012Beltrán Flórez, LJ, Acosta Cárdenas, A. . Empleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosuero. Hechos Microbiol. 2012; 3(2);25-35.2145-8898http://hdl.handle.net/10495/101932805-6485ABSTRACT: The whey is the largest waste subproduct of the dairy industry. Due to its high values of BOD is considered a source of water and soil contamination when discarded without any treatment. An alternative for the disposal of this agroindustrial waste is its application as a culture medium for various fermentation processes after an enzymatic hydrolysis thus ensuring a greater availability of fermentable sugars for subsequent application in biotechnology, environment and / or food. Objective To evaluate the effects of pH, temperature and enzyme concentration on whey using a commercial β-galactosidase from Kluyveromyces lactis, and determine the kinetic parameters of the enzyme. Materials and methods The hydrolysis of lactose was performed in buffered solutions of lactose and in whey as well, 5 levels were evaluated for pH (4.5-8.5), temperature (25°C-65°C) and enzyme concentration (0.025 g/L to 0.5 g/L), all the experiments were performed in triplicate in Erlenmeyer flask (100 mL) and analyzed using the GraphPad Prism software. Results We found that the best conditions of pH and temperature for the whey hydrolysis were at 6,5°C and 45°C respectively. According to the kinetic results, the enzyme presented competitive inhibition for galactose with a Km equal to 8.01x10-2 M, Ki of 6.85x10-2 M and Vmax of 1.86x10-2 molmg-1min-1. Conclusions The best conditions of pH and temperature were 6.5°C and 45°C respectively, a 100% of hydrolysis was achieved in one hour with 0.1 g/L of enzyme. Furthermore, it was shown that the reaction rate of the enzyme is inhibited by galactose.RESUMEN: El lactosuero es el mayor subproducto de desecho de la industria láctea. Por sus elevados valores de DBO se considera un foco de contaminación de aguas y suelo cuando se descarta sin ningún tratamiento. Una alternativa para la disposición final de este residuo agroindustrial, es su utilización como medio de cultivo para varios procesos fermentativos, después de una hidrólisis enzimática, de esta manera garantizar una mayor disponibilidad de azucares fermentables, para su posterior aplicación en biotecnología, medio ambiente y/o alimentos. Objetivo Evaluar los efectos del pH, temperatura y concentración de la enzima sobre lactosuero empleando una β-galactosidasa comercial de Kluyveromyces lactis y determinar los parámetros cinéticos de la enzima. Materiales y métodos La hidrólisis de la lactosa se desarrolló tanto en soluciones tamponadas de lactosa como en lactosuero, se evaluaron 5 niveles para el pH (4,5 - 8,5), temperatura (25°C-65°C) y concentración de enzima (0,025 g/L - 0,5 g/L), todos los experimentos se realizaron por triplicado en matraz de 100 mL y los datos fueron analizados empleando el software GraphPad Prism. Resultados A un pH de 6,5 y una temperatura de 45°C, se alcanzaron las mejores condiciones de hidrolisis del lactosuero. De acuerdo a los resultados cinéticos, la enzima presentó inhibición competitiva por galactosa con un Km igual a 8,01x10-2M, Ki de 6,85x10-2M y Vmax de 1,86x10-2molmg-1min-1. Conclusión Las mejores condiciones de temperatura y pH fueron de 6,5°C y 45°C respectivamente, se alcanzó un 100% de hidrólisis en una hora con 0,1 g/L de enzima. Además, se evidenció que la velocidad de reacción de la enzima fue inhibida por galactosa.COL0066991application/pdfspaUniversidad de Antioquia, Escuela de MicrobiologíaGrupo de BiotransformaciónMedellín, Colombiainfo: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-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/Beta-GalactosidasaGalactosidasaHidrólisis enzimáticaKluyveromycesLactosueroSuero de lecheEnzymatic hydrolysisWheyEmpleo de una ß-galactosidasa comercial de Kluyveromyces lactis en la hidrólisis de lactosueroUsage of a commercial β-galactosidase from Kluyveromyces lactis in the hydrolysis of wheyHechos Microbiol.Hechos Microbiológicos253532ORIGINALBeltranLaura_2012_GalactosidasacomercialHidrolisis.pdfBeltranLaura_2012_GalactosidasacomercialHidrolisis.pdfArtículo de investigaciónapplication/pdf412744http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/1/BeltranLaura_2012_GalactosidasacomercialHidrolisis.pdfad9614ba0a7ee70353aa6f6699292484MD51CC-LICENSElicense_urllicense_urltext/plain; charset=utf-849http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/2/license_url4afdbb8c545fd630ea7db775da747b2fMD52license_textlicense_texttext/html; charset=utf-80http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/3/license_textd41d8cd98f00b204e9800998ecf8427eMD53license_rdflicense_rdfLicenciaapplication/rdf+xml; charset=utf-80http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/4/license_rdfd41d8cd98f00b204e9800998ecf8427eMD54LICENSElicense.txtlicense.txttext/plain; charset=utf-81748http://bibliotecadigital.udea.edu.co/bitstream/10495/10193/5/license.txt8a4605be74aa9ea9d79846c1fba20a33MD5510495/10193oai:bibliotecadigital.udea.edu.co:10495/101932022-04-22 10:16:02.444Repositorio Institucional Universidad de Antioquiaandres.perez@udea.edu.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 |