Programa Institucional de Fomento a la Investigación, Desarrollo e Innovación, Universidad Tecnológica Metropolitana, Ignacio Valdivieso 2409, San Joaquín, Santiago, Chile.
IONCHEM Ltda, Avda. Diego Portales 925, 301, Viña del Mar, Chile.
J Biotechnol. 2020 Feb 20;310:97-102. doi: 10.1016/j.jbiotec.2020.02.003. Epub 2020 Feb 6.
The immobilization of lipases in cross linked aggregates (CLEA) leads to a robust biocatalyst that remains very stable in low viscous non-conventional Deep Eutectic Solvents - Buffer mixtures. To reinforce that stability, and to facilitate the biocatalyst recovery, this paper explores the immobilization of Lipase-CLEA derivatives in Lentikats®. This double immobilization can be successfully used in esterifications in DES-buffer media, using substrates of unpaired solubilities (e.g. benzoic acid and glycerol), in batch and continuous processes, and reaching full conversion. Under these conditions, the derivatives display an improved stability (compared to the Lipase-CLEA derivatives) and enable the reuse of the reaction media in continuous devices for at least 6 cycles under non-optimized conditions, accumulating 10 g product L, enhancing the productivity, and opening exciting future options for sustainable chemistry.
脂肪酶的固定化交联聚集体（CLEA）形成了一种坚固的生物催化剂，在低粘度非常规深共晶溶剂-缓冲混合体系中非常稳定。为了增强这种稳定性，并便于生物催化剂的回收，本文探索了脂肪酶-CLEA 衍生物在 Lentikats®中的固定化。这种双重固定化可成功用于 DES-缓冲介质中的酯化反应，使用非配对溶解度的底物（例如苯甲酸和甘油），在间歇和连续过程中，达到完全转化。在这些条件下，与脂肪酶-CLEA 衍生物相比，衍生物显示出更好的稳定性，并能使反应介质在非优化条件下连续使用至少 6 个循环，积累 10 g 产物 L，提高了生产力，并为可持续化学开辟了令人兴奋的未来选择。
