Improved Performance of Magnetic Cross-Linked Lipase Aggregates by Interfacial Activation: A Robust and Magnetically Recyclable Biocatalyst for Transesterification of Jatropha Oil.
Improved Performance of Magnetic Cross-Linked Lipase Aggregates by Interfacial Activation: A Robust and Magnetically Recyclable Biocatalyst for Transesterification of Jatropha Oil.
复制标题
DOI：
10.3390/molecules22122157
复制
发表时间：
2017-12-07
期刊：
影响因子：
--
通讯作者：
Yu X
中科院分区：
文献类型：
--
作者：
Zhang W;Yang H;Liu W;Wang N;Yu X
脂肪酶是商业工业中最广泛使用的酶。大多数脂肪酶的催化机制涉及称为“界面活化”的步骤。由于界面活化可以显著提高催化活性，因此在脂肪酶固定化方法的研究中具有重要意义。为了获得一种具有工业化生产生物柴油潜力的生物催化剂，提出了一种提高固定化脂肪酶催化活性和稳定性的有效方法。这是通过将界面活化与混合磁性交联脂肪酶聚集体相结合来进行的。以米黑根毛霉脂肪酶（RML）为固定化底物，研究了该催化剂的固定化性能.在最佳条件下，表面活性剂活化的磁性RML交联酶聚集体（CLEA）的活性回收率高达2058%，与游离RML相比提高了20倍。此外，固定化的RML表现出优异的催化性能的生物柴油反应的产率为93%，更重要的是，可以很容易地从反应混合物中分离，通过简单的磁倾析，并保留超过84%的初始活性后，5个实例的重复使用。本研究为设计和制备高活性、高稳定性的固定化脂肪酶提供了一条新的途径。
Lipases are the most widely employed enzymes in commercial industries. The catalytic mechanism of most lipases involves a step called “interfacial activation”. As interfacial activation can lead to a significant increase in catalytic activity, it is of profound importance in developing lipase immobilization methods. To obtain a potential biocatalyst for industrial biodiesel production, an effective strategy for enhancement of catalytic activity and stability of immobilized lipase was developed. This was performed through the combination of interfacial activation with hybrid magnetic cross-linked lipase aggregates. This biocatalyst was investigated for the immobilization of lipase from Rhizomucor miehei (RML). Under the optimal conditions, the activity recovery of the surfactant-activated magnetic RML cross-linked enzyme aggregates (CLEAs) was as high as 2058%, with a 20-fold improvement over the free RML. Moreover, the immobilized RML showed excellent catalytic performance for the biodiesel reaction at a yield of 93%, and more importantly, could be easily separated from the reaction mixture by simple magnetic decantation, and retained more than 84% of its initial activities after five instances of reuse. This study provides a new and versatile approach for designing and fabricating immobilized lipase with high activation and stability.
登录
查看更多内容
影响因子：
5.5
作者：
Adrio JL;Demain AL
通讯作者：
Demain AL
影响因子：
10.4
作者：
Amini, Zeynab;Ilham, Zul;Chen, Wei-Hsin
通讯作者：
Chen, Wei-Hsin
影响因子：
3.6
作者：
Huang, Ze-Lin;Yang, Tao-Xiang;Yang, Zhen
通讯作者：
Yang, Zhen
影响因子：
1.7
作者：
Jääskeläinen, S;Verma, CS;Caves, LSD
通讯作者：
Caves, LSD
影响因子：
--
作者：
Secundo, F;Carrea, G;Eggert, T
通讯作者：
Eggert, T