Hybridization of Homogeneous and Heterogeneous Catalysis to Develop a Novel Biocatalyst via Immobilization of Lipase on Surface Modified Mesoporous Silica Towards Biodiesel Synthesis Application

To achieve carbon neutrality, biodiesel blending in diesel has attracted attention due to its advantages, such as its production of less particulate matter and its sulphur‐free nature. Transesterification reaction (of vegetable oil, used cooking oil, and/or animal fats) is the most common route to biodiesel synthesis. However, reported catalysts for transesterification generally suffer disadvantages such as difficult product separation, low conversion, and low yields in biodiesel. In present study, to address these issues, a novel biocatalyst is developed via immobilization of Candida Antarctica Lipase B (CAL‐B) on both SBA‐15 and 3‐(methacryloyloxy)propyltrimethoxysilane (MPS/MP‐Silane) surface‐modified SBA‐15 to form CAL‐B/(MP‐)SBA‐15 and utilized for transesterification of triacetin, a model compound for biodiesel synthesis. Effect of biocatalyst parameters such as surface modification, mesopore size, enzyme loading, and thermal stability is studied to optimize the catalyst performance. As a result, high enzyme loading of up to 75 wt% and tenfold increase in enzymatic hydrolysis activity are achieved for CAL‐B/MP‐SBA‐15 (12 nm). Moreover, CAL‐B/SBA‐15 (8 nm) is found to catalyze the transesterification of triacetin in up to 100% conversion with 99% yield of methyl acetate. Thermal stability of catalysts is observed even at 80 °C with increased enzymatic activities. The results propose CAL‐B/SBA‐15 (8 nm) as a potential candidate for biodiesel synthesis.