Creating a new biocatalytic complex with extremolipases and biocompatible ionic liquids for improved transesterification reactions

The ongoing energy crisis has spurred increased research into sustainable and more competitive methods for producing biofuels, including biodiesel. In this context, the focus of the current study is to underscore the viability of investing in a novel biocatalytic complex. This complex incorporates e...

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Bibliographic Details
Published in:Energy Conversion and Management: X
Main Authors: L. González, María S. Álvarez, Ana Rodríguez, María A. Longo, Francisco J. Deive
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier 2023
Subjects:
Online Access:https://doi.org/10.1016/j.ecmx.2023.100456
https://doaj.org/article/7e8732392e2f4d73b60761b6777c972c
Description
Summary:The ongoing energy crisis has spurred increased research into sustainable and more competitive methods for producing biofuels, including biodiesel. In this context, the focus of the current study is to underscore the viability of investing in a novel biocatalytic complex. This complex incorporates extremophilic lipases and biocompatible ionic liquids with the aim of achieving exceptionally high conversions in transesterification reactions without generating glycerol. Through a meticulous screening process encompassing various amino acid and dipeptide-based ionic liquids from the ammonium family, cholinium glycinate turned out to be the optimal choice. This selection was driven not only by its enhanced compatibility with a commercially available Candida antarctica lipase B (CaLB) but also with extremophilic enzymes synthesized in-house, derived from halophilic (Halomonas spLM1C) and thermophilic (Thermus thermophilus HB27) strains. Following rigorous testing of both free and immobilized enzymes, the ideal concentration of the ionic liquid in transesterification reactions was determined to be 1% relative to the sunflower oil content. Comparative analysis of conversion rates between immobilized thermophilic lipase and immobilized CaLB revealed the efficacy of the proposed approach. Maximum conversions were found to increase by 20%, with specific conversion rates soaring by approximately 180% when utilizing the immobilized thermophilic lipase. In conclusion, this research ushers in new prospects for advancing the competitiveness of biocatalytic solutions in glycerol-free transesterification reactions, underscoring its potential to revolutionize the landscape of sustainable energy production.