Biodiesel serves as a crucial biofuel alternative to petroleum-based diesel fuels, achieved through enzymatic transesterification of oil substrates. This study aims to investigate stabilized lipase (LP) within calcium carbonate (CaCO3) microparticles as a catalyst for solvent-free transesterification in biodiesel synthesis. The specific hydrolysis activity of the in-situ immobilized LP was 66% of that of free LP. However, the specific transesterification activity of immobilized LP in the solvent-free phase for biodiesel production was 2.29 times higher than that of free LP. These results suggest that the interfacial activation of LP molecules is facilitated by the inorganic CaCO3 environment. The immobilized LP demonstrated higher biodiesel production levels with superior stability compared to free LP, particularly regarding methanol molar ratio and temperature. To the best of our knowledge, there are no previous reports on the in-situ immobilization of LP in a CaCO3 carrier without any crosslinker as an interfacial-activated biocatalyst for biodiesel production.

中文翻译：

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碳酸钙微粒中的原位稳定脂肪酶，用于生物柴油生产无溶剂酯交换反应中的活化


生物柴油是石油基柴油燃料的重要生物燃料替代品，通过油底物的酶促酯交换反应实现。本研究旨在研究碳酸钙 (CaCO3) 微粒内的稳定脂肪酶 (LP) 作为生物柴油合成中无溶剂酯交换反应的催化剂。原位固定化LP的比水解活性是游离LP的66%。然而，用于生物柴油生产的无溶剂相固定化LP的比酯交换活性比游离LP高2.29倍。这些结果表明，无机 CaCO3 环境促进了 LP 分子的界面活化。与游离LP相比，固定化LP表现出更高的生物柴油产量水平和优异的稳定性，特别是在甲醇摩尔比和温度方面。据我们所知，之前还没有关于在不使用任何交联剂的情况下将LP原位固定在CaCO3载体中作为界面活化生物催化剂用于生物柴油生产的报道。