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Título: | Immobilized forms of the ophiostoma piceae lipase for green synthesis of biodiesel. Comparison with eversa transform 2.0 and Cal A |
Autor: | Molina-Gutiérrez, María CSIC; Alcaraz, Lorena; López Gómez, Félix Antonio CSIC ORCID CVN ; Rodríguez-Sánchez, Leonor CSIC ; Martínez, María Jesús CSIC ORCID ; Prieto Orzanco, Alicia CSIC ORCID | Palabras clave: | Biocatalysis Transesterification Recycled oil FAMEs Sustainability |
Fecha de publicación: | 2021 | Editor: | Multidisciplinary Digital Publishing Institute | Citación: | Journal of Fungi 7 (10): 822 (2021) | Resumen: | 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. | Versión del editor: | https://doi.org/10.3390/jof7100822 | URI: | http://hdl.handle.net/10261/258081 | DOI: | 10.3390/jof7100822 | Identificadores: | doi: 10.3390/jof7100822 issn: 2309-608X |
Aparece en las colecciones: | (CENIM) Artículos (CIB) Artículos |
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