Zhao Bin, Liu Xinlong, Jiang Yanjun, Zhou Liya, He Ying, Gao Jing
School of Chemical Engineering and Technology, Hebei University of Technology, Tianjin, 300130, China.
Appl Biochem Biotechnol. 2014 Aug;173(7):1802-14. doi: 10.1007/s12010-014-0967-2. Epub 2014 May 31.
Lipase Candida sp. 99-125 has been proved to be quite effective in catalyzing organic synthesis reactions and is much cheaper than commercial lipases. Mesoporous silicates are attractive materials for the immobilization of enzymes due to their unique structures. The present research designed a hydrophobic silicate with uniform pore size suitable for the comfort of lipase Candida sp. 99-125 for improving its activity and stability. The resulting immobilized lipase (LP@PMO) by adsorption was employed to catalyze hydrolysis, esterification, and transesterification reactions, and the performances were compared with the lipase immobilized on hydrophilic silicate (LP@PMS) and native lipase. The LP@PMO showed as high activity as that of native lipase in hydrolysis and much increased catalytic activity and reusability in the reactions for biodiesel production. Besides, LP@PMO also possessed better organic stability. Such results demonstrate that immobilization of lipase onto hydrophobic supports is a promising strategy to fabricate highly active and stable biocatalysts for applications.
假丝酵母脂肪酶99 - 125已被证明在催化有机合成反应方面相当有效，且比商业脂肪酶便宜得多。介孔硅酸盐因其独特的结构而成为固定化酶的有吸引力的材料。本研究设计了一种孔径均匀的疏水硅酸盐，以适配假丝酵母脂肪酶99 - 125，从而提高其活性和稳定性。通过吸附得到的固定化脂肪酶（LP@PMO）用于催化水解、酯化和酯交换反应，并将其性能与固定在亲水性硅酸盐上的脂肪酶（LP@PMS）和天然脂肪酶进行比较。LP@PMO在水解反应中表现出与天然脂肪酶一样高的活性，并且在生物柴油生产反应中具有显著提高的催化活性和可重复使用性。此外，LP@PMO还具有更好的有机稳定性。这些结果表明，将脂肪酶固定在疏水载体上是制备用于应用的高活性和稳定生物催化剂的一种有前景的策略。
