Department of Chemical Engineering, Institute of Chemical Technology, Matunga (E), Mumbai 400019, India.
Department of Chemical Engineering, Institute of Chemical Technology, Matunga (E), Mumbai 400019, India.
Int J Biol Macromol. 2020 Jun 1;152:1108-1112. doi: 10.1016/j.ijbiomac.2019.10.199. Epub 2019 Nov 18.
The immobilization of enzyme with enhanced catalytic activity is the major challenge. In this work, we have activated the lipase in the presence of proline and successfully immobilized into zeolitic imidazolate framework (ZIF)-8 by biomineralization method. The prepared lipase-proline MOF exhibited 135% enhanced catalytic activity as compared to free counterpart. Further, it exhibited four-fold improved thermal stability with respect to native enzyme after immobilization. In Michaelis-Menten kinetic studies, K values for lipase-proline MOF were found to be lower, whereas, it exhibited higher V than lipase-MOF and free lipase. The lipase-MOF and lipase-proline MOF were showed 56% and 72% residual activity, respectively after six cycles of reuse.
提高酶催化活性的固定化是主要挑战。在这项工作中，我们在脯氨酸存在的情况下激活了脂肪酶，并通过生物矿化法成功地将其固定到沸石咪唑酯骨架（ZIF）-8 中。与游离酶相比，制备的脂肪酶-脯氨酸 MOF 表现出 135%的增强催化活性。此外，与天然酶相比，固定化后其热稳定性提高了四倍。在米氏动力学研究中，发现脂肪酶-脯氨酸 MOF 的 K 值较低，而 V 值高于脂肪酶-MOF 和游离脂肪酶。脂肪酶-MOF 和脂肪酶-脯氨酸 MOF 在重复使用六次后分别表现出 56%和 72%的残留活性。
