Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry
ABSTRACT: Banana peel after chemical ant thermal modification was used as an alternative support to immobilize the commercial enzyme naringinase (Penicillum Decumbens); an immobilization yields greater than 70% was observed at pH 7. The structural characteristics of the support were determined by sc...
- Autores:
-
Mediavilla Quintero, Marta Beatriz
Caicedo Paz, Angie Vanessa
Villa Holguín, Aída Luz
Martínez Galán, Julián Paul
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2023
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/43514
- Acceso en línea:
- https://hdl.handle.net/10495/43514
- Palabra clave:
- Enzimas
Enzymes
Enzimas Inmovilizadas
Enzymes, Immobilized
Naringinasa
Naringinase
https://id.nlm.nih.gov/mesh/D004798
https://id.nlm.nih.gov/mesh/D004800
- Rights
- openAccess
- License
- https://creativecommons.org/licenses/by/4.0/
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| dc.title.spa.fl_str_mv |
Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry |
| dc.title.translated.spa.fl_str_mv |
Naringinasa inmovilizada en cáscara de plátano modificada con posible aplicación en la industria de los cítricos |
| title |
Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry |
| spellingShingle |
Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry Enzimas Enzymes Enzimas Inmovilizadas Enzymes, Immobilized Naringinasa Naringinase https://id.nlm.nih.gov/mesh/D004798 https://id.nlm.nih.gov/mesh/D004800 |
| title_short |
Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry |
| title_full |
Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry |
| title_fullStr |
Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry |
| title_full_unstemmed |
Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry |
| title_sort |
Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry |
| dc.creator.fl_str_mv |
Mediavilla Quintero, Marta Beatriz Caicedo Paz, Angie Vanessa Villa Holguín, Aída Luz Martínez Galán, Julián Paul |
| dc.contributor.author.none.fl_str_mv |
Mediavilla Quintero, Marta Beatriz Caicedo Paz, Angie Vanessa Villa Holguín, Aída Luz Martínez Galán, Julián Paul |
| dc.contributor.researchgroup.spa.fl_str_mv |
Alimentación y Nutrición Humana Catálisis Ambiental |
| dc.subject.decs.none.fl_str_mv |
Enzimas Enzymes Enzimas Inmovilizadas Enzymes, Immobilized |
| topic |
Enzimas Enzymes Enzimas Inmovilizadas Enzymes, Immobilized Naringinasa Naringinase https://id.nlm.nih.gov/mesh/D004798 https://id.nlm.nih.gov/mesh/D004800 |
| dc.subject.proposal.spa.fl_str_mv |
Naringinasa Naringinase |
| dc.subject.meshuri.none.fl_str_mv |
https://id.nlm.nih.gov/mesh/D004798 https://id.nlm.nih.gov/mesh/D004800 |
| description |
ABSTRACT: Banana peel after chemical ant thermal modification was used as an alternative support to immobilize the commercial enzyme naringinase (Penicillum Decumbens); an immobilization yields greater than 70% was observed at pH 7. The structural characteristics of the support were determined by scanning electron microscopy with elemental analysis, showing the presence of pores and elements such as carbon, oxygen, sulfur, and zinc, while the attachment of the enzyme was concluded by infrared spectroscopy. For the free and immobilized enzyme, the KM and Vmax values were 0.0006 molar and 2000 U, and 0.0003 molar and 1666 U, respectively. The temperatures of the greatest activity for the free was 70°C and for the immobilized enzyme was 50°C, respectively, and the best pH was 4.5 in both cases. It was found that, after the third use, the catalyst maintained 50% of the enzymatic activity. These results seem to suggest the potential of the synthesized material for its application in the debittering of citrus juices. |
| publishDate |
2023 |
| dc.date.issued.none.fl_str_mv |
2023 |
| dc.date.accessioned.none.fl_str_mv |
2024-11-15T20:34:53Z |
| dc.date.available.none.fl_str_mv |
2024-11-15T20:34:53Z |
| 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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Mediavilla Quintero M-B, Caicedo Paz A-V, Villa Holguín AL, Martínez Galán J-P. Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry. Ing. Investig. Desarr. [Internet]. 25 de junio de 2023 [citado 28 de junio de 2024];23(1):33-42. Disponible en: https://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/15844 |
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1900-771X |
| dc.identifier.uri.none.fl_str_mv |
https://hdl.handle.net/10495/43514 |
| dc.identifier.doi.none.fl_str_mv |
10.19053/1900771X.v23.n1.2023.15844 |
| dc.identifier.eissn.none.fl_str_mv |
2422-4324 |
| identifier_str_mv |
Mediavilla Quintero M-B, Caicedo Paz A-V, Villa Holguín AL, Martínez Galán J-P. Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry. Ing. Investig. Desarr. [Internet]. 25 de junio de 2023 [citado 28 de junio de 2024];23(1):33-42. Disponible en: https://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/15844 1900-771X 10.19053/1900771X.v23.n1.2023.15844 2422-4324 |
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https://hdl.handle.net/10495/43514 |
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eng |
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eng |
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Ing. Investig. Desarr. |
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42 |
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1 |
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33 |
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23 |
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Ingeniería, Investigación y Desarrollo |
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10 páginas |
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application/pdf |
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Universidad Pedagógica y Tecnológica de Colombia |
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Sogamoso, Colombia |
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Universidad de Antioquia |
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Mediavilla Quintero, Marta BeatrizCaicedo Paz, Angie VanessaVilla Holguín, Aída LuzMartínez Galán, Julián PaulAlimentación y Nutrición HumanaCatálisis Ambiental2024-11-15T20:34:53Z2024-11-15T20:34:53Z2023Mediavilla Quintero M-B, Caicedo Paz A-V, Villa Holguín AL, Martínez Galán J-P. Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus Industry. Ing. Investig. Desarr. [Internet]. 25 de junio de 2023 [citado 28 de junio de 2024];23(1):33-42. Disponible en: https://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/158441900-771Xhttps://hdl.handle.net/10495/4351410.19053/1900771X.v23.n1.2023.158442422-4324ABSTRACT: Banana peel after chemical ant thermal modification was used as an alternative support to immobilize the commercial enzyme naringinase (Penicillum Decumbens); an immobilization yields greater than 70% was observed at pH 7. The structural characteristics of the support were determined by scanning electron microscopy with elemental analysis, showing the presence of pores and elements such as carbon, oxygen, sulfur, and zinc, while the attachment of the enzyme was concluded by infrared spectroscopy. For the free and immobilized enzyme, the KM and Vmax values were 0.0006 molar and 2000 U, and 0.0003 molar and 1666 U, respectively. The temperatures of the greatest activity for the free was 70°C and for the immobilized enzyme was 50°C, respectively, and the best pH was 4.5 in both cases. It was found that, after the third use, the catalyst maintained 50% of the enzymatic activity. These results seem to suggest the potential of the synthesized material for its application in the debittering of citrus juices.RESUMEN: La cáscara de plátano después de una modificación térmica química se utilizó como soporte alternativo para inmovilizar la enzima comercial naringinasa (Penicillum Decumbens); se observaron rendimientos de inmovilización superiores al 70% a pH 7. Las características estructurales del soporte se determinaron mediante microscopía electrónica de barrido con análisis elemental, evidenciándose la presencia de poros y elementos como carbono, oxígeno, azufre y zinc, mientras que la unión de la enzima se concluyó mediante espectroscopia infrarroja. Para la enzima libre e inmovilizada, los valores de KM y Vmax fueron 0,0006 molar y 2000 U, y 0,0003 molar y 1666 U, respectivamente. Las temperaturas de mayor actividad para la enzima libre fue 70°C y para la inmovilizada fue 50°C, respectivamente, y el mejor pH fue 4,5 en ambos casos. Se encontró que, después del tercer uso, el catalizador mantuvo el 50% de la actividad enzimática. Estos resultados parecen sugerir el potencial del material sintetizado para su aplicación en el desamargado de jugos de cítricos.Universidad de Antioquia. Vicerrectoría de investigación. Comité para el Desarrollo de la Investigación - CODIColombia. Ministerio de Ciencia, Tecnología e Innovación - MinCienciasColombia. Ministerio de Educación Nacional - MinEducaciónColombia. Ministerio de Comercio, Industria y Turismo - MinCITICETEX (Instituto Colombiano de Crédito Educativo y Estudios Técnicos en el Exterior)COL0000407COL000194110 páginasapplication/pdfengUniversidad Pedagógica y Tecnológica de ColombiaSogamoso, Colombiahttps://creativecommons.org/licenses/by/4.0/http://creativecommons.org/licenses/by/2.5/co/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Naringinase Immobilized on Modified Banana Peel with Potential Application in the Citrus IndustryNaringinasa inmovilizada en cáscara de plátano modificada con posible aplicación en la industria de los cítricosArtículo 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/publishedVersionEnzimasEnzymesEnzimas InmovilizadasEnzymes, ImmobilizedNaringinasaNaringinasehttps://id.nlm.nih.gov/mesh/D004798https://id.nlm.nih.gov/mesh/D004800Ing. Investig. 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