In this work, we analyzed the suitability of a versatile recombinant lipase, secreted by Ophiostoma piceae (OPEr) and produced in Pichia pastoris, as a catalyst of the synthesis of biodiesel. The enzyme was immobilized by five covalent procedures and by hydrophobicity on functionalized nanoparticles of magnetite or of a novel Zn/Mn oxide named G1. Then, they were tested for green production of biodiesel by solventless enzymatic transesterification of discarded cooking oil and methanol (1:4) at 25 °C. The results were compared with those shown by free OPEr and the commercial lipases Eversa® and Cal A®. Several preparations with immobilized OPEr produced high synthesis yields (>90% transesterification), comparable to those obtained with Eversa®, the commercial enzyme designed for this application. Three of the biocatalysts maintained their catalytic efficiency for nine cycles. The process catalyzed by AMNP-CH-OPEr was scaled from 500 μL to 25 mL (50 times), improving its efficiency.
CITATION STYLE
Molina-Gutiérrez, M., Alcaraz, L., López, F. A., Rodríguez-Sánchez, L., Martínez, M. J., & Prieto, A. (2021). Immobilized forms of the ophiostoma piceae lipase for green synthesis of biodiesel. Comparison with eversa transform 2.0 and Cal A. Journal of Fungi, 7(10). https://doi.org/10.3390/jof7100822
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