CINDECA   05422
CENTRO DE INVESTIGACION Y DESARROLLO EN CIENCIAS APLICADAS "DR. JORGE J. RONCO"
Unidad Ejecutora - UE
artículos
Título:
Novozym 435: THE PERFECT LIPASE IMMOBILIZED BIOCATALYST?
Autor/es:
FERREIRA, MARÍA LUJÁN; RODRIGUES, RAFAEL C; FERNANDEZ-LAFUENTE, ROBERTO; BARBOSA, OVEIMAR; BERENGUER-MURCIA, ÁNGEL; ORTIZ, CLAUDIA; DOS SANTOS, JOSE C. S.; BRIAND, LAURA ESTEFANIA
Revista:
Catalysis Science & Technology
Editorial:
Royal Society of Chemistry
Referencias:
Lugar: CAmbridge; Año: 2019 vol. 9 p. 2380 - 2420
ISSN:
2044-4753
Resumen:
Novozym 435 (N435) is a commercially available immobilized lipase produced byNovozymes. It is based on the immobilization via interfacial activation of the lipase B from Candidaantarctica on a resin, Lewatit VP OC 1600. This resin is a macroporous support formed bypoly(methyl methacrylate) crosslinked with divinylbenzene. N435 is perhaps the most widely usedcommercial biocatalyst in both academy and industry. Here, we review some of the success stories ofN435 (in chemistry, energy and lipid manipulation), but we focus on some of the problems that the useof this biocatalyst may generate. Some of these problems are just based on the mechanism ofimmobilization (interfacial activation) that may facilitate enzyme desorption under certain conditions.Other problems are specific to the support: mechanical fragility, moderate hydrophilicity that permitsthe accumulation of hydrophilic compounds (e.g., water or glycerin) and the most critical one, supportdissolution in some organic media. Finally, some solutions (N435 coating with silicone, enzymephysical or chemical crosslinking, use of alternative supports) are proposed. However N435 history,even with these problems, may continue in the coming future due to its very good properties if somesimpler alternative biocatalyst is not developed