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: | , , , , , , , |
Other Authors: | , , , , , , , , , , , , , |
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Royal Society of Chemistry (UK)
2019
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Online Access: | http://hdl.handle.net/10261/229588 https://doi.org/10.1039/c9cy00415g https://doi.org/10.13039/501100003359 https://doi.org/10.13039/501100002923 https://doi.org/10.13039/501100003339 https://doi.org/10.13039/501100004263 https://doi.org/10.13039/501100005283 https://doi.org/10.13039/501100003074 |
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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. We gratefully recognize the financial support from MINECO from the Spanish Government (project number CTQ2017-86170-R, Colciencias, Ministerio de Educación Nacional, Ministerio de Industria, Comercio y Turismo e ICETEX, Convocatoria Ecosistema Científico – Colombia Científica. Fondo Francisco José de Caldas, Contrato RC-FP44842-212-2018 and Colciencias (Colombia) (project number FP44842-076-2016), Generalitat Valenciana (PROMETEO/2018/076), FAPERGS (project number 17/2551-0000939-8), CONICET (R. Argentina), FUNCAP (project number BP3-0139-00005.01.00/18) and ANPCyT (PICT 2015-0932 and PICT CABBIO 4687). We acknowledge support of the publication fee by the CSIC Open Access Support Initiative through its Unit of ... |
author2 |
Ministerio de Ciencia, Innovación y Universidades (España) Ministerio de Industria, Comercio y Turismo (España) Colciencias (Colombia) Generalitat Valenciana Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina) Consejo Superior de Investigaciones Científicas (España) Ministerio de Educación Nacional (Colombia) ICETEX (Colombia) Fondo Francisco José de Caldas Fundação de Amparo à Pesquisa do Estado do Rio Grande do Sul Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico Agencia Nacional de Promoción Científica y Tecnológica (Argentina) Dos Santos, José C. S Berenguer-Murcia, Ánge Briand, Laura E. Fernández-Lafuente, Roberto |
format |
Article in Journal/Newspaper |
author |
Ortiz, Claudia Ferreira, María Luján Barbosa, Oveimar Dos Santos, José C. S. Rodrigues, Rafael C. Berenguer-Murcia, Ángel Briand, Laura E. Fernández-Lafuente, Roberto |
spellingShingle |
Ortiz, Claudia Ferreira, María Luján Barbosa, Oveimar Dos Santos, José C. S. Rodrigues, Rafael C. Berenguer-Murcia, Ángel Briand, Laura E. Fernández-Lafuente, Roberto Novozym 435: The "perfect" lipase immobilized biocatalyst? |
author_facet |
Ortiz, Claudia Ferreira, María Luján Barbosa, Oveimar Dos Santos, José C. S. Rodrigues, Rafael C. Berenguer-Murcia, Ángel Briand, Laura E. Fernández-Lafuente, Roberto |
author_sort |
Ortiz, Claudia |
title |
Novozym 435: The "perfect" lipase immobilized 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? |
publisher |
Royal Society of Chemistry (UK) |
publishDate |
2019 |
url |
http://hdl.handle.net/10261/229588 https://doi.org/10.1039/c9cy00415g https://doi.org/10.13039/501100003359 https://doi.org/10.13039/501100002923 https://doi.org/10.13039/501100003339 https://doi.org/10.13039/501100004263 https://doi.org/10.13039/501100005283 https://doi.org/10.13039/501100003074 |
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Argentina |
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Antarc* Antarctica |
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Antarc* Antarctica |
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#PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/CTQ2017-86170-R Publisher's version http://dx.doi.org/10.1039/c9cy00415g Sí doi:10.1039/c9cy00415g issn: 2044-4753 e-issn: 2044-4761 Catalysis Science and Technology 9(10): 2380-2420 (2019) http://hdl.handle.net/10261/229588 http://dx.doi.org/10.13039/501100003359 http://dx.doi.org/10.13039/501100002923 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100004263 http://dx.doi.org/10.13039/501100005283 http://dx.doi.org/10.13039/501100003074 |
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https://doi.org/10.1039/c9cy00415g10.13039/50110000335910.13039/50110000292310.13039/50110000333910.13039/50110000426310.13039/50110000528310.13039/501100003074 |
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Catalysis Science & Technology |
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ftcsic:oai:digital.csic.es:10261/229588 2024-02-11T09:58:42+01:00 Novozym 435: The "perfect" lipase immobilized biocatalyst? Ortiz, Claudia Ferreira, María Luján Barbosa, Oveimar Dos Santos, José C. S. Rodrigues, Rafael C. Berenguer-Murcia, Ángel Briand, Laura E. Fernández-Lafuente, Roberto Ministerio de Ciencia, Innovación y Universidades (España) Ministerio de Industria, Comercio y Turismo (España) Colciencias (Colombia) Generalitat Valenciana Consejo Nacional de Investigaciones Científicas y Técnicas (Argentina) Consejo Superior de Investigaciones Científicas (España) Ministerio de Educación Nacional (Colombia) ICETEX (Colombia) Fondo Francisco José de Caldas Fundação de Amparo à Pesquisa do Estado do Rio Grande do Sul Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico Agencia Nacional de Promoción Científica y Tecnológica (Argentina) Dos Santos, José C. S Berenguer-Murcia, Ánge Briand, Laura E. Fernández-Lafuente, Roberto 2019-05-21 http://hdl.handle.net/10261/229588 https://doi.org/10.1039/c9cy00415g https://doi.org/10.13039/501100003359 https://doi.org/10.13039/501100002923 https://doi.org/10.13039/501100003339 https://doi.org/10.13039/501100004263 https://doi.org/10.13039/501100005283 https://doi.org/10.13039/501100003074 unknown Royal Society of Chemistry (UK) #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/CTQ2017-86170-R Publisher's version http://dx.doi.org/10.1039/c9cy00415g Sí doi:10.1039/c9cy00415g issn: 2044-4753 e-issn: 2044-4761 Catalysis Science and Technology 9(10): 2380-2420 (2019) http://hdl.handle.net/10261/229588 http://dx.doi.org/10.13039/501100003359 http://dx.doi.org/10.13039/501100002923 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100004263 http://dx.doi.org/10.13039/501100005283 http://dx.doi.org/10.13039/501100003074 open artículo de revisión http://purl.org/coar/resource_type/c_dcae04bc 2019 ftcsic https://doi.org/10.1039/c9cy00415g10.13039/50110000335910.13039/50110000292310.13039/50110000333910.13039/50110000426310.13039/50110000528310.13039/501100003074 2024-01-16T11:02:49Z 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. We gratefully recognize the financial support from MINECO from the Spanish Government (project number CTQ2017-86170-R, Colciencias, Ministerio de Educación Nacional, Ministerio de Industria, Comercio y Turismo e ICETEX, Convocatoria Ecosistema Científico – Colombia Científica. Fondo Francisco José de Caldas, Contrato RC-FP44842-212-2018 and Colciencias (Colombia) (project number FP44842-076-2016), Generalitat Valenciana (PROMETEO/2018/076), FAPERGS (project number 17/2551-0000939-8), CONICET (R. Argentina), FUNCAP (project number BP3-0139-00005.01.00/18) and ANPCyT (PICT 2015-0932 and PICT CABBIO 4687). We acknowledge support of the publication fee by the CSIC Open Access Support Initiative through its Unit of ... Article in Journal/Newspaper Antarc* Antarctica Digital.CSIC (Spanish National Research Council) Argentina Catalysis Science & Technology 9 10 2380 2420 |