Enhanced fatty acid production using recombinant Lipase in a Rotating Bed Reactor (RBR)

This study investigated the immobilization of recombinant lipase onto modified Nickel foam to enhance enzyme lifespan and reusability in palm oil hydrolysis. Nickel foam, with its high porosity and extensive surface area, provides optimal support for enzyme catalysis, facilitating enhanced substrate-enzyme interaction. Employing Nickel foam as an immobilization matrix for lipase within a Rotating Bed Reactor (RBR) offers a novel method to optimize fatty acid production. Physicochemical analysis confirmed a 97.45 % immobilization yield and 74.93 % retention of its initial activity, demonstrating efficient immobilization and stability. The turnover frequency (TOF) of the immobilized lipase increased with rotation speed, achieving an optimal 55.38 % fatty acid conversion at 600 rpm over 9 hours. Compared to the free enzyme, the immobilized form showed notable thermal stability, retaining 85.40 % activity after two days at 60 °C, and maintained performance over six reuse cycles. Furthermore, the immobilized lipase required 3.82 times less enzyme to achieve the same amount of product as the free enzyme. These findings highlight the potential of Nickel foam as an effective support for His-tagged enzymes, significantly enhancing durability and reusability in palm oil hydrolysis, thus supporting more efficient fatty acid production.