dc.creatorOrtiz, Claudia Susana
dc.creatorFerreira, María Luján
dc.creatorBarbosa, Oveimar
dc.creatordos Santos, Jose C. S.
dc.creatorRodrigues, Rafael C.
dc.creatorBerenguer Murcia, Ángel
dc.creatorBriand, Laura Estefania
dc.creatorFernandez Lafuente, Roberto
dc.date.accessioned2021-09-28T18:34:26Z
dc.date.accessioned2022-10-15T12:18:56Z
dc.date.available2021-09-28T18:34:26Z
dc.date.available2022-10-15T12:18:56Z
dc.date.created2021-09-28T18:34:26Z
dc.date.issued2019-04-12
dc.identifierOrtiz, 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
dc.identifier2044-4753
dc.identifierhttp://hdl.handle.net/11336/141746
dc.identifier2044-4761
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4385164
dc.description.abstractNovozym 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.
dc.languageeng
dc.publisherRoyal Society of Chemistry
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2019/CY/C9CY00415G
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1039/C9CY00415G
dc.rightshttps://creativecommons.org/licenses/by-nc/2.5/ar/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectLIPASE
dc.subjectNOVOZYM 435
dc.subjectSUPPORT BREAKAGE
dc.subjectENZYME LEACHING
dc.titleNovozym 435: The "perfect" lipase immobilized biocatalyst?
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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