Stabilization of immobilized lipases by treatment with metallic phosphate salts

• Published in: International Journal of Biological Macromolecules
• Main Authors: Guimarães, José R., Carballares, Diego, Rocha Martin, Javier, Tardioli, Paulo W., Fernandez-Lafuente, Roberto
• Format: Article in Journal/Newspaper
• Language: English
• Published: Elsevier 2022
• Subjects: Bioquímica; Rugosa; Antarc*; Antarctica
• Online Access: https://eprints.ucm.es/id/eprint/75130/; https://eprints.ucm.es/id/eprint/75130/1/Guimar%C3%A4es,%20JR.%20et%20al.%202022.%20Stabilization%20of%20immobilized%20lipases%20by%20treatment.pdf; https://doi.org/10.1016/j.ijbiomac.2022.05.167

Lipases from Thermomyces lanuginosus (TLL), Rhizomucor miehei (RML), Candida rugosa (CRL), forms A and B of lipase from Candida antarctica (CALA and CALB) and Eversa Transform 2.0 have been immobilized on octyl-agarose beads at two different loads (1 mg/g and saturated support) and treated with phosphate and/or some metallic salts (Zn2+, Co2+, Cu2+). They have been also immobilized on the support modified by the metallic phosphate, usually driving to biocatalyst with lower stability or marginal improvements. The effects of the phosphate/metal modification on enzyme features depended on the loading of the support. Some enzymes (TLL, CRL or CALA), mainly using the highly loaded biocatalysts, showed very significant improvement on enzyme stability after the treatment with some of the metal phosphates (next to a 20-fold factor), improvements that were not justified by the presence of metallic or phosphate ions in solution, as they had negative effects on enzyme stabilities. In some other cases, a significant increase in enzyme activity was detected (e.g., CALB). This could be explained by the modification of the nucleation places of the enzymes by the metallic phosphate, and this could help to explain the good results obtained in the nanoflower immobilization of many enzymes.