Novozym 435: the “perfect” lipase immobilized biocatalyst?

• Published in: Catalysis Science & Technology
• Main Authors: Ortiz, Claudia, Luján Ferreira, María, Barbosa, Oveimar, Santos, Jose Cleiton S. dos, Rodrigues, Rafael C., Berenguer-Murcia, Ángel, Briand, Laura E., Fernández Lafuente, Roberto
• Other Authors: Universidad de Alicante. Departamento de Química Inorgánica, Universidad de Alicante. Instituto Universitario de Materiales, Materiales Carbonosos y Medio Ambiente
• Format: Article in Journal/Newspaper
• Language: English
• Published: Royal Society of Chemistry 2019
• Subjects: Novozym 435; Immobilized lipase; Biocatalyst; Química Inorgánica; Argentina; Antarc*; Antarctica
• Online Access: http://hdl.handle.net/10045/93828; https://doi.org/10.1039/C9CY00415G

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).