Key Laboratory of Biomass Chemical Engineering of Ministry of Education, Department of Chemical and Biological Engineering, Zhejiang University, Hangzhou, 310027, China.
Appl Biochem Biotechnol. 2019 Jul;188(3):677-689. doi: 10.1007/s12010-018-02947-2. Epub 2019 Jan 8.
Nano-sized FeO was synthesized by chemical co-precipitation and subsequently modified with 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde to introduce aldehyde group on its surface. With the help of "interface activation" by adding sucrose esters-11 as surfactant, lipase from Rhizopus oryzae was successfully immobilized onto the carrier with great enhancement of activity. The hydrolysis activity of immobilized enzyme were 9.16 times and 31.6 times of free enzyme when p-nitrophenol butyrate and p-nitrophenol palmitate were used as substrates. The thermo-stability of immobilized enzyme was also enhanced compared to free enzyme. The immobilized enzyme was successfully applied in synthesis of 1,3-diacyglycerols (1,3-DAG). The specific esterification activity of immobilized enzyme was about 1.5 times of the free enzyme. The immobilized enzyme showed good region-selectivity towards 1,3-diacyglycerols and retained nearly 80% of its activity after reused for 60 times, revealing a good industrial application prospect.
纳米级 FeO 通过化学共沉淀法合成,随后用 3-氨丙基三乙氧基硅烷(APTES)和戊二醛改性,在其表面引入醛基。通过添加蔗糖酯-11 作为表面活性剂进行“界面活化”,成功地将米根霉脂肪酶固定在载体上,大大提高了其活性。当以丁酸对硝基苯酚酯和棕榈酸对硝基苯酚酯作为底物时,固定化酶的水解活性分别是游离酶的 9.16 倍和 31.6 倍。与游离酶相比,固定化酶的热稳定性也得到了提高。固定化酶成功地应用于 1,3-二酰基甘油(1,3-DAG)的合成。固定化酶的酯化活性约为游离酶的 1.5 倍。固定化酶对 1,3-二酰基甘油具有良好的区域选择性,重复使用 60 次后仍保留近 80%的活性,显示出良好的工业应用前景。