Sun Nan,Wu Qing,Jin Lifang,Zhu Zichen,Sun Jianhui,Dong Shuying,Xie Haijiao,Zhang Chunyan,Cui Yanrui
By using a two-step hydrothermal method and trithiocyanuric acid (TTCA), 2,4,6-trihydrazino-1,3,5-triazine (THT), and Fe 3 O 4 as raw materials, a spherical magnetic adsorbent polymer (TTCA/THT@Fe 3 O 4 ) was synthesized to achieve the efficient removal of Cr(VI) from wastewater. Under optimal adsorption conditions, the maximum adsorption capacity of TTCA/THT@Fe 3 O 4 for Cr(VI) can reach 1340 mg·g −1 . Notably, the removal efficiency can approach 98.9%, even at the lower concentration of 20 mg·L −1 Cr(VI). For actual wastewater containing Cr(VI), the Cr(VI) concentration was reduced from 25.8 to 0.4 mg·L −1 , a remarkable 20% lower than the current industry discharge standard value. A mechanism for the high adsorption performance of Cr(VI) on TTCA/THT@Fe 3 O 4 was investigated using Fourier transform infrared spectroscopy, X-ray photoelectron spectroscopy, and density functional theory. It can be plausibly attributed to the formation of Cr/N and Cr/S coordination bonds. Additionally, surface electrostatic adsorption, reduction effects, and the spherical polymer structure increase the contact area with Cr(VI), maximizing adsorption. The synergistic effect of adsorption and reduction enhances the adsorption performance of TTCA/THT@Fe 3 O 4 for Cr(VI) and total chromium in water. The resultant polymer has a simple preparation process, excellent adsorption performance, easy magnetic separation, and promising application for actual wastewater.
The functionalized modification of proteins from more sustainable resources is urgently required. Herein, the fibrillization of oilseed proteins derived from different sources was conducted, and the conformation-fibrillization relationship was further elaborated by systematically comparing the physicochemical and functional properties of amyloid fibrils. The results indicated that fibrillization-induced alterations in particle size and ζ-potential, ThT fluorescence intensity, surface hydrophobicity, flexibility and rheological property differed among proteins due to their diverse proportions of secondary structure and subunit compositions. Compared with soy proteins, walnut proteins were more likely to be hydrolyzed into peptides with a smaller particle size (108.6 nm) and fibrillated at a higher conversion rate (65.4%). The sesame proteins featured by a higher level of β-sheet exhibited increased surface hydrophobicity and flexibility of fibrils, resulting in higher viscosity due to the formation of cluster-like fibrillar aggregates. The rapeseed protein fibrils derived from cruciferin and napin demonstrated the lower digestibility (20.51%) as they displayed strong resistance against acid and proteolytic digestion during in-vitro digestion. Furthermore, among four oilseed proteins, short-flexible fibrils from sesame and walnut proteins could adhere firmly to oil/water interface, maintaining a gel-like structure of HIPEs with excellent printing accuracy and high self-supporting capacity.
危险品化学品经营许可证（带存储）