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
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/144001

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network_name_str SEDICI (UNLP)
spelling 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
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/144001
url http://sedici.unlp.edu.ar/handle/10915/144001
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/issn/2044-4761
info:eu-repo/semantics/altIdentifier/doi/10.1039/c9cy00415g
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc/4.0/
Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc/4.0/
Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
dc.format.none.fl_str_mv application/pdf
2380-2420
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
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instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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