NARINGINASE IMMOBILIZED ON MODIFIED BANANA PEEL WITH POTENTIAL APPLICATION IN THE CITRUS INDUSTRY

Banana peel after chemical ant thermal modification was used as an alternative support to immobilize the commercial enzyme naringinase (Penicillum Decumbens); an immobilization yield greater than 70% was observed at pH 7. The morphology of the support was characterized by scanning electron microscop...

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Autores:
Tipo de recurso:
http://purl.org/coar/resource_type/c_6783
Fecha de publicación:
2023
Institución:
Universidad Pedagógica y Tecnológica de Colombia
Repositorio:
RiUPTC: Repositorio Institucional UPTC
Idioma:
eng
OAI Identifier:
oai:repositorio.uptc.edu.co:001/12372
Acceso en línea:
https://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/15844
https://repositorio.uptc.edu.co/handle/001/12372
Palabra clave:
Enzyme
Immobilization
Naringinase
enzyme
immobilization
naringinase
Rights
License
Derechos de autor 2023 Ingeniería Investigación y Desarrollo
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spelling 2023-06-252024-07-05T18:48:13Z2024-07-05T18:48:13Zhttps://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/1584410.19053/1900771X.v23.n1.2023.15844https://repositorio.uptc.edu.co/handle/001/12372Banana peel after chemical ant thermal modification was used as an alternative support to immobilize the commercial enzyme naringinase (Penicillum Decumbens); an immobilization yield greater than 70% was observed at pH 7. The morphology of the support was characterized by scanning electron microscopy with elemental analysis, showing the presence of pores and elements such as carbon, oxygen, sulfur, and zinc, while the immobilization of the enzyme was confirmed by infrared spectroscopy. For the free and immobilized enzyme, the KM and Vmax values were 0.0006 mg/mL and 2000 U, and 0.0003 mg/mL and 1666 U, respectively. The temperatures of greatest activity for the free and immobilized enzyme were 70°C and 50°C, respectively, and the optimum 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 food industry, specifically; in the debittering of citrus juices.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.application/pdfengengUniversidad Pedagógica y Tecnológica de Colombia - UPTChttps://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/15844/13025Derechos de autor 2023 Ingeniería Investigación y Desarrollohttp://purl.org/coar/access_right/c_abf284http://purl.org/coar/access_right/c_abf2Ingeniería Investigación y Desarrollo; Vol. 23 No. 1 (2023): January - June; 33 - 42Ingeniería Investigación y Desarrollo; Vol. 23 Núm. 1 (2023): Enero - Junio; 33 - 422422-43241900-771XEnzymeImmobilizationNaringinaseenzymeimmobilizationnaringinaseNARINGINASE IMMOBILIZED ON MODIFIED BANANA PEEL WITH POTENTIAL APPLICATION IN THE CITRUS INDUSTRYNaringinase immobilized on modified banana peel with potential application in the citrus industryinfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6783http://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a367http://purl.org/coar/version/c_970fb48d4fbd8a85Mediavilla Quintero, Marta-BeatrizCaicedo Paz, Angie-VanessaVilla Holguín, Aida LuzMartínez Galán, Julián-Paul001/12372oai:repositorio.uptc.edu.co:001/123722025-07-18 11:25:54.33metadata.onlyhttps://repositorio.uptc.edu.coRepositorio Institucional UPTCrepositorio.uptc@uptc.edu.co
dc.title.en-US.fl_str_mv NARINGINASE IMMOBILIZED ON MODIFIED BANANA PEEL WITH POTENTIAL APPLICATION IN THE CITRUS INDUSTRY
dc.title.es-ES.fl_str_mv Naringinase immobilized on modified banana peel with potential application in the citrus industry
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
Enzyme
Immobilization
Naringinase
enzyme
immobilization
naringinase
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.subject.en-US.fl_str_mv Enzyme
Immobilization
Naringinase
topic Enzyme
Immobilization
Naringinase
enzyme
immobilization
naringinase
dc.subject.es-ES.fl_str_mv enzyme
immobilization
naringinase
description Banana peel after chemical ant thermal modification was used as an alternative support to immobilize the commercial enzyme naringinase (Penicillum Decumbens); an immobilization yield greater than 70% was observed at pH 7. The morphology of the support was characterized by scanning electron microscopy with elemental analysis, showing the presence of pores and elements such as carbon, oxygen, sulfur, and zinc, while the immobilization of the enzyme was confirmed by infrared spectroscopy. For the free and immobilized enzyme, the KM and Vmax values were 0.0006 mg/mL and 2000 U, and 0.0003 mg/mL and 1666 U, respectively. The temperatures of greatest activity for the free and immobilized enzyme were 70°C and 50°C, respectively, and the optimum 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 food industry, specifically; in the debittering of citrus juices.
publishDate 2023
dc.date.accessioned.none.fl_str_mv 2024-07-05T18:48:13Z
dc.date.available.none.fl_str_mv 2024-07-05T18:48:13Z
dc.date.none.fl_str_mv 2023-06-25
dc.type.none.fl_str_mv info:eu-repo/semantics/article
dc.type.coar.fl_str_mv http://purl.org/coar/resource_type/c_2df8fbb1
dc.type.coarversion.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.coar.spa.fl_str_mv http://purl.org/coar/resource_type/c_6783
dc.type.coarversion.spa.fl_str_mv http://purl.org/coar/version/c_970fb48d4fbd8a367
format http://purl.org/coar/resource_type/c_6783
dc.identifier.none.fl_str_mv https://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/15844
10.19053/1900771X.v23.n1.2023.15844
dc.identifier.uri.none.fl_str_mv https://repositorio.uptc.edu.co/handle/001/12372
url https://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/15844
https://repositorio.uptc.edu.co/handle/001/12372
identifier_str_mv 10.19053/1900771X.v23.n1.2023.15844
dc.language.none.fl_str_mv eng
dc.language.iso.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv https://revistas.uptc.edu.co/index.php/ingenieria_sogamoso/article/view/15844/13025
dc.rights.es-ES.fl_str_mv Derechos de autor 2023 Ingeniería Investigación y Desarrollo
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.coar.spa.fl_str_mv http://purl.org/coar/access_right/c_abf284
rights_invalid_str_mv Derechos de autor 2023 Ingeniería Investigación y Desarrollo
http://purl.org/coar/access_right/c_abf284
http://purl.org/coar/access_right/c_abf2
dc.format.none.fl_str_mv application/pdf
dc.publisher.es-ES.fl_str_mv Universidad Pedagógica y Tecnológica de Colombia - UPTC
dc.source.en-US.fl_str_mv Ingeniería Investigación y Desarrollo; Vol. 23 No. 1 (2023): January - June; 33 - 42
dc.source.es-ES.fl_str_mv Ingeniería Investigación y Desarrollo; Vol. 23 Núm. 1 (2023): Enero - Junio; 33 - 42
dc.source.none.fl_str_mv 2422-4324
1900-771X
institution Universidad Pedagógica y Tecnológica de Colombia
repository.name.fl_str_mv Repositorio Institucional UPTC
repository.mail.fl_str_mv repositorio.uptc@uptc.edu.co
_version_ 1839633897849094144

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