Candida rugosa lipase covalently immobilized on facilely-synthesized carbon nitride nanosheets as a novel biocatalyst
文献类型: 外文期刊
第一作者: Li, Ya
作者: Li, Ya;Zheng, Mingming;Deng, Qianchun;Zhang, Shan;Zheng, Chang;Tang, Hu;Huang, Fenghong;Shi, Jie;Ruan, Zhijun
作者机构:
期刊名称:RSC ADVANCES ( 影响因子:3.361; 五年影响因子:3.39 )
ISSN: 2046-2069
年卷期: 2018 年 8 卷 26 期
页码:
收录情况: SCI
摘要: The immobilization of lipase on solid supports provides a significant improvement to the stability and reusability of lipase. During immobilization, the restricted surface area and inferior separation capacity of matrix materials are crucial for obtaining high-quality immobilized lipase. Carbon nitride nanosheets (C3N4-NS) as a type of two-dimensional nanomaterial have attracted various attentions for their prominent 2D planar nanostructure, characteristic surface area, thermostability and biocompatibility. Herein, we report a rational design and fabrication of immobilized Candida rugosa lipase based on carbon nitride nanosheets (C3N4-NS) as the matrix. The synthetic C3N4-NS are characterized by transmission electron microscopy, Brunauer-Emmett-Teller gas sorptometry measurement, X-ray powder diffraction, Fourier transform infrared spectroscopy and thermogravimetric analysis. These results show that C3N4-NS possess an as-expected two-dimensional nanostructure with a large surface area of 74.374 m(2) g(-1). In addition, we chose glutaraldehyde-assisted covalent attachment to combine C3N4-NS and Candida rugosa lipase (CRL) via amino groups at the margins of C3N4-NS. The as-constructed immobilized lipase (C3N4-NS@CRL) exhibits satisfactory enzyme-loading (44.76 mg g(-1)), pH-flexibility, thermostability (after 180 min at 50 degrees C, 67% of the initial activity remained) and recyclability (after 10 runs, 72% of the initial activity remained). When compared with the free CRL, all experimental data indicate that C3N4-NS@CRL exhibited improved stability and enhanced practicability. To our knowledge, this is the first report of the application of carbon nitride nanosheets to enzyme immobilization.
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