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<p>Developing thermally stable, reusable enzymes is key to eco-friendly biodiesel production. Here, we report the first immobilization of a sequence-reconstructed ancestral lipase from family 1.3 lipase, last universal common ancestor (LUCA) onto Seplite LX120, a cross-linked styrene–divinylbenzene resin, via a simple physical adsorption strategy. The immobilized LUCA exhibited broad operational stability, maintaining over 80% activity from 20–100&#xa0;°C and above 50% across pH 4–9, with optimal performance at 70&#xa0;°C (565.48 U/g) and pH 9 (534.52 U/g). Enhanced solvent and storage stability were observed compared to the free enzyme, with over 50% residual activity after 12&#xa0;weeks at 4&#xa0;°C and excellent tolerance in polar solvents. Notably, the biocatalyst retained 95.35% activity after 10 reuse cycles. Characterization by Scanning Electron Microscopy (SEM) revealed enzyme coverage on the Seplite LX120 surface, while Brunauer–Emmett–Teller (BET) analysis confirmed suitable surface area and porosity for effective immobilization. Both free and immobilized LUCA catalyzed efficient transesterification of waste cooking oil (WCO), yielding 95% and 100% biodiesel, respectively, within 3&#xa0;h under optimized conditions: methanol-to-oil molar ratio of 6:1, shaking at 150&#xa0;rpm, and 70&#xa0;°C. These findings highlight the promise of ancestral enzyme immobilization as a novel route to high-performance, sustainable biocatalysts for biodiesel synthesis from low-cost feedstocks.</p> Graphical Abstract <p></p> <p>Summary of biodiesel transesterification using immobilized and free LUCA lipase (Created with&#xa0;BioRender.com)</p>

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Immobilized Ancient Lipase for Waste-to-Fuel Biocatalysis: Toward Sustainable Biodiesel Production

  • 期刊论文

  • 发表日期：

    2025年11月19日

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  • Afifah Husna Mat Saad,
  • Nor Hafizah Ahmad Kamarudin,
  • Adam Thean Chor Leow,
  • Mohd Shamzi Mohamed,
  • Mohd Shukuri Mohamad Ali

摘要

Developing thermally stable, reusable enzymes is key to eco-friendly biodiesel production. Here, we report the first immobilization of a sequence-reconstructed ancestral lipase from family 1.3 lipase, last universal common ancestor (LUCA) onto Seplite LX120, a cross-linked styrene–divinylbenzene resin, via a simple physical adsorption strategy. The immobilized LUCA exhibited broad operational stability, maintaining over 80% activity from 20–100 °C and above 50% across pH 4–9, with optimal performance at 70 °C (565.48 U/g) and pH 9 (534.52 U/g). Enhanced solvent and storage stability were observed compared to the free enzyme, with over 50% residual activity after 12 weeks at 4 °C and excellent tolerance in polar solvents. Notably, the biocatalyst retained 95.35% activity after 10 reuse cycles. Characterization by Scanning Electron Microscopy (SEM) revealed enzyme coverage on the Seplite LX120 surface, while Brunauer–Emmett–Teller (BET) analysis confirmed suitable surface area and porosity for effective immobilization. Both free and immobilized LUCA catalyzed efficient transesterification of waste cooking oil (WCO), yielding 95% and 100% biodiesel, respectively, within 3 h under optimized conditions: methanol-to-oil molar ratio of 6:1, shaking at 150 rpm, and 70 °C. These findings highlight the promise of ancestral enzyme immobilization as a novel route to high-performance, sustainable biocatalysts for biodiesel synthesis from low-cost feedstocks.

Graphical Abstract

Summary of biodiesel transesterification using immobilized and free LUCA lipase (Created with BioRender.com)