Novozym 435: The "perfect" lipase immobilized biocatalyst?

• Published in: Catalysis Science & Technology
• Main Authors: Ortiz, Claudia, Ferreira, María Luján, Barbosa, Oveimar, Dos Santos, José C. S., Rodrigues, Rafael C., Berenguer-Murcia, Ángel, Briand, Laura E., Fernández-Lafuente, Roberto
• Other Authors: 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
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: Royal Society of Chemistry (UK) 2019
• Subjects: Argentina; Antarc*; Antarctica
• 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

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 ...