Novozym 435: The "perfect" lipase immobilized biocatalyst?
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 poly(methyl methacrylate) crosslinked wi...
Published in: | Catalysis Science & Technology |
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Main Authors: | , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
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Royal Society of Chemistry
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Online Access: | http://hdl.handle.net/11336/141746 |
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author | Ortiz, Claudia Susana Ferreira, María Luján Barbosa, Oveimar dos Santos, Jose C. S. Rodrigues, Rafael C. Berenguer Murcia, Ángel Briand, Laura Estefania Fernandez Lafuente, Roberto |
author_facet | Ortiz, Claudia Susana Ferreira, María Luján Barbosa, Oveimar dos Santos, Jose C. S. Rodrigues, Rafael C. Berenguer Murcia, Ángel Briand, Laura Estefania Fernandez Lafuente, Roberto |
author_sort | Ortiz, Claudia Susana |
collection | CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
container_issue | 10 |
container_start_page | 2380 |
container_title | Catalysis Science & Technology |
container_volume | 9 |
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 poly(methyl 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. Fil: Ortiz, Claudia Susana. Universidad Industrial Santander; Colombia Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina Fil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas; Colombia Fil: dos Santos, Jose C. S. Universidade Da Integracao Internacional Da Lusofonia Afrobrasileira.; Brasil Fil: Rodrigues, Rafael C. Universidade Federal do Rio Grande do Sul; Brasil Fil: Berenguer Murcia, Ángel. Universidad de Alicante. Facultad de Ciencias. Departamento de Quimica Inorganica.; España ... |
format | Article in Journal/Newspaper |
genre | Antarc* Antarctica |
genre_facet | Antarc* Antarctica |
geographic | Argentina Ortiz Ferreira |
geographic_facet | Argentina Ortiz Ferreira |
id | ftconicet:oai:ri.conicet.gov.ar:11336/141746 |
institution | Open Polar |
language | English |
long_lat | ENVELOPE(-59.717,-59.717,-62.450,-62.450) ENVELOPE(-62.050,-62.050,-64.600,-64.600) |
op_collection_id | ftconicet |
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op_doi | https://doi.org/10.1039/C9CY00415G |
op_relation | info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2019/CY/C9CY00415G info:eu-repo/semantics/altIdentifier/doi/10.1039/C9CY00415G http://hdl.handle.net/11336/141746 Ortiz, Claudia Susana; Ferreira, María Luján; Barbosa, Oveimar; dos Santos, Jose C. S.; Rodrigues, Rafael C.; et al.; Novozym 435: The "perfect" lipase immobilized biocatalyst?; Royal Society of Chemistry; Catalysis Science and Technology; 9; 10; 12-4-2019; 2380-2420 2044-4753 2044-4761 CONICET Digital CONICET |
op_rights | info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc/2.5/ar/ |
publisher | Royal Society of Chemistry |
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spelling | ftconicet:oai:ri.conicet.gov.ar:11336/141746 2025-01-16T19:23:14+00:00 Novozym 435: The "perfect" lipase immobilized biocatalyst? Ortiz, Claudia Susana Ferreira, María Luján Barbosa, Oveimar dos Santos, Jose C. S. Rodrigues, Rafael C. Berenguer Murcia, Ángel Briand, Laura Estefania Fernandez Lafuente, Roberto application/pdf http://hdl.handle.net/11336/141746 eng eng Royal Society of Chemistry info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2019/CY/C9CY00415G info:eu-repo/semantics/altIdentifier/doi/10.1039/C9CY00415G http://hdl.handle.net/11336/141746 Ortiz, Claudia Susana; Ferreira, María Luján; Barbosa, Oveimar; dos Santos, Jose C. S.; Rodrigues, Rafael C.; et al.; Novozym 435: The "perfect" lipase immobilized biocatalyst?; Royal Society of Chemistry; Catalysis Science and Technology; 9; 10; 12-4-2019; 2380-2420 2044-4753 2044-4761 CONICET Digital CONICET info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc/2.5/ar/ LIPASE NOVOZYM 435 SUPPORT BREAKAGE ENZYME LEACHING https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1039/C9CY00415G 2023-09-24T19:58:11Z 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 poly(methyl 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. Fil: Ortiz, Claudia Susana. Universidad Industrial Santander; Colombia Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina Fil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas; Colombia Fil: dos Santos, Jose C. S. Universidade Da Integracao Internacional Da Lusofonia Afrobrasileira.; Brasil Fil: Rodrigues, Rafael C. Universidade Federal do Rio Grande do Sul; Brasil Fil: Berenguer Murcia, Ángel. Universidad de Alicante. Facultad de Ciencias. Departamento de Quimica Inorganica.; España ... Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Ortiz ENVELOPE(-59.717,-59.717,-62.450,-62.450) Ferreira ENVELOPE(-62.050,-62.050,-64.600,-64.600) Catalysis Science & Technology 9 10 2380 2420 |
spellingShingle | LIPASE NOVOZYM 435 SUPPORT BREAKAGE ENZYME LEACHING https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 Ortiz, Claudia Susana Ferreira, María Luján Barbosa, Oveimar dos Santos, Jose C. S. Rodrigues, Rafael C. Berenguer Murcia, Ángel Briand, Laura Estefania Fernandez Lafuente, Roberto Novozym 435: The "perfect" lipase immobilized biocatalyst? |
title | 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_short | Novozym 435: The "perfect" lipase immobilized biocatalyst? |
title_sort | novozym 435: the "perfect" lipase immobilized biocatalyst? |
topic | LIPASE NOVOZYM 435 SUPPORT BREAKAGE ENZYME LEACHING https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
topic_facet | LIPASE NOVOZYM 435 SUPPORT BREAKAGE ENZYME LEACHING https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
url | http://hdl.handle.net/11336/141746 |