Novozym 435: the “perfect” lipase immobilized biocatalyst?
- Autores
- Ortiz, Claudia; Ferreira, María Luján; Barbosa, Oveimar; Dos Santos, José C. S.; Rodrigues, Rafael C.; Berenguer Murcia, Ángel; Briand, Laura Estefanía; Fernandez Lafuente, Roberto
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida antarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed by polyIJmethyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely used commercial biocatalyst in both academy and industry. Here, we review some of the success stories of N435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the use of this biocatalyst may generate. Some of these problems are just based on the mechanism of immobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions. Other problems are specific to the support: mechanical fragility, moderate hydrophilicity that permits the accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, support dissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzyme physical or chemical crosslinking, and use of alternative supports) are proposed. However, the N435 history, even with these problems, may continue in the coming future due to its very good properties if some simpler alternative biocatalysts are not developed.
Centro de Investigación y Desarrollo en Ciencias Aplicadas - Materia
-
Química
Lipase
Novozym 435
Biocatalyst - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/144001
Ver los metadatos del registro completo
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Novozym 435: the “perfect” lipase immobilized biocatalyst?Ortiz, ClaudiaFerreira, María LujánBarbosa, OveimarDos Santos, José C. S.Rodrigues, Rafael C.Berenguer Murcia, ÁngelBriand, Laura EstefaníaFernandez Lafuente, RobertoQuímicaLipaseNovozym 435BiocatalystNovozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida antarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed by polyIJmethyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely used commercial biocatalyst in both academy and industry. Here, we review some of the success stories of N435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the use of this biocatalyst may generate. Some of these problems are just based on the mechanism of immobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions. Other problems are specific to the support: mechanical fragility, moderate hydrophilicity that permits the accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, support dissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzyme physical or chemical crosslinking, and use of alternative supports) are proposed. However, the N435 history, even with these problems, may continue in the coming future due to its very good properties if some simpler alternative biocatalysts are not developed.Centro de Investigación y Desarrollo en Ciencias Aplicadas2019-05-20info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf2380-2420http://sedici.unlp.edu.ar/handle/10915/144001enginfo:eu-repo/semantics/altIdentifier/issn/2044-4753info:eu-repo/semantics/altIdentifier/issn/2044-4761info:eu-repo/semantics/altIdentifier/doi/10.1039/c9cy00415ginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc/4.0/Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:04:23Zoai:sedici.unlp.edu.ar:10915/144001Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:04:23.382SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Novozym 435: the “perfect” lipase immobilized biocatalyst? |
title |
Novozym 435: the “perfect” lipase immobilized biocatalyst? |
spellingShingle |
Novozym 435: the “perfect” lipase immobilized biocatalyst? Ortiz, Claudia Química Lipase Novozym 435 Biocatalyst |
title_short |
Novozym 435: the “perfect” lipase immobilized biocatalyst? |
title_full |
Novozym 435: the “perfect” lipase immobilized biocatalyst? |
title_fullStr |
Novozym 435: the “perfect” lipase immobilized biocatalyst? |
title_full_unstemmed |
Novozym 435: the “perfect” lipase immobilized biocatalyst? |
title_sort |
Novozym 435: the “perfect” lipase immobilized biocatalyst? |
dc.creator.none.fl_str_mv |
Ortiz, Claudia Ferreira, María Luján Barbosa, Oveimar Dos Santos, José C. S. Rodrigues, Rafael C. Berenguer Murcia, Ángel Briand, Laura Estefanía Fernandez Lafuente, Roberto |
author |
Ortiz, Claudia |
author_facet |
Ortiz, Claudia Ferreira, María Luján Barbosa, Oveimar Dos Santos, José C. S. Rodrigues, Rafael C. Berenguer Murcia, Ángel Briand, Laura Estefanía Fernandez Lafuente, Roberto |
author_role |
author |
author2 |
Ferreira, María Luján Barbosa, Oveimar Dos Santos, José C. S. Rodrigues, Rafael C. Berenguer Murcia, Ángel Briand, Laura Estefanía Fernandez Lafuente, Roberto |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Química Lipase Novozym 435 Biocatalyst |
topic |
Química Lipase Novozym 435 Biocatalyst |
dc.description.none.fl_txt_mv |
Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida antarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed by polyIJmethyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely used commercial biocatalyst in both academy and industry. Here, we review some of the success stories of N435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the use of this biocatalyst may generate. Some of these problems are just based on the mechanism of immobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions. Other problems are specific to the support: mechanical fragility, moderate hydrophilicity that permits the accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, support dissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzyme physical or chemical crosslinking, and use of alternative supports) are proposed. However, the N435 history, even with these problems, may continue in the coming future due to its very good properties if some simpler alternative biocatalysts are not developed. Centro de Investigación y Desarrollo en Ciencias Aplicadas |
description |
Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida antarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed by polyIJmethyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely used commercial biocatalyst in both academy and industry. Here, we review some of the success stories of N435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the use of this biocatalyst may generate. Some of these problems are just based on the mechanism of immobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions. Other problems are specific to the support: mechanical fragility, moderate hydrophilicity that permits the accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, support dissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzyme physical or chemical crosslinking, and use of alternative supports) are proposed. However, the N435 history, even with these problems, may continue in the coming future due to its very good properties if some simpler alternative biocatalysts are not developed. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-05-20 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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http://sedici.unlp.edu.ar/handle/10915/144001 |
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http://sedici.unlp.edu.ar/handle/10915/144001 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
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openAccess |
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http://creativecommons.org/licenses/by-nc/4.0/ Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0) |
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