| Literature DB >> 35386065 |
Hui Peng1,2,3, Wenge Dong2, Qiwei Chen2, Haiyan Song1,2,3, Hongxu Sun2, Ren Li1,2,3, Yanhong Chang4,5, Hui Luo6.
Abstract
In this study, nitrilase (Nit) was immobilized in zeolite imidazole framework-90 (ZIF-90) by one-pot biomimetic mineralization strategy. The structure, morphology and functional groups of ZIF-90 and immobilized enzyme Nit@ZIF-90 were characterized by scanning electron microscopy (SEM)/energy-dispersive X-ray spectroscopy (EDX), transmission electron microscopy (TEM), X-ray diffraction (XRD), thermogravimetric analysis (TGA) and Fourier transform infrared spectroscopy (FT-IR). Circular dichroism (CD) proved that the immobilized method of encapsulation in ZIF-90 could effectively maintain the intrinsic conformation of Nit. Meanwhile, the stability and reusability of Nit@ZIF-90 were systematically evaluated. Compared with the free enzyme, the thermal, pH and organic solvents stability of Nit@ZIF-90 were significantly increased. Further, Nit@ZIF-90 exhibited better reusability during the hydrolysis of acrylonitrile and retained 48.34% of the initial activity after 10 cycles. Besides, the Ni@ZIF-90 had preferable storage stability, which showed a high degree of residual activity (more than 64 %) after storage at 4 °C for 7 d. The improved stability and reusability of the Nit@ZIF-90 implied that it could be used as a potential effective biocatalyst for hydrolysis of nitrile compounds in industrial application.Entities:
Keywords: biomimetic mineralization; immobilization; nitrilase; reusability; stability; zeolite imidazole framework
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Year: 2022 PMID: 35386065 DOI: 10.1007/s12010-022-03890-z
Source DB: PubMed Journal: Appl Biochem Biotechnol ISSN: 0273-2289 Impact factor: 3.094