不同的蛋白質具有不同的等電點,因此調控蛋白質水溶液的酸鹼值可以改變蛋白質的帶電性質。本論文以具有陰離子交換能力的鋰-鋁層狀雙氫氧化合物( Li-Al Layered Double Hydroxides, Li-Al LDH )作為吸附蛋白質的載體,因此能夠透過載體和不同蛋白質吸附能力的差異性達到分離之應用。 本研究對鋰-鋁層狀雙氫氧化合物進行醋酸活化的改質反應,以改善其對特定蛋白質之吸附能力。並對改質前、後的層狀雙氫氧化合物以X-光繞射儀、孔洞及表面積分析儀、紅外線光譜儀、固態核磁共振儀的鋰譜、鋁譜、碳譜、氫譜、元素分析儀、場發式電子顯微鏡以及膨潤度檢測完成材料的性質鑑定,當鋰-鋁層狀雙氫氧化合物進行醋酸改質後,其在水溶液的膨潤度提升了25 %。 由於層板的主結構,以氫氧化鋁為主要組成,當改質前、後的層狀雙氫氧化合物個別吸附牛血清蛋白( Bovine Serum Albumin, BSA )或雞蛋白溶菌酶( Lysozyme ),再以紫外光-可見光光譜儀檢測,材料改質後能吸附最多的BSA量為383.1 mg/ g以及最少的Lysozyme量12.8 mg/ g。並且針對改質後的材料與BSA對飽和吸附度探討,其次以氯化鈉或磷酸緩衝溶液做脫附BSA的比較,最後探討此材料重複吸、脫附的生命週期。最後,將BSA和Lysozyme混合後測試,並藉由十二烷基硫酸鈉聚丙烯醯胺凝膠電泳檢測,吸附後之水溶液僅存有Lysozyme,脫附後也能將BSA脫出,因此說明層狀雙氫氧化合物具蛋白質純化的應用潛力。
Different proteins have different isoelectrical points; therefore, the charge property of the protein may be changed through the controlling of pH in the solution. In this thesis, the lithium- aluminum layered double hydroxide compound (Li-Al Layered Double Hydroxides, Li-Al LDH), with the anion exchange capacity, would be the adsorbent template for carrier of the protein. It is possible through the carrier and the differences in protein adsorption ability to achieve the separation and purification of proteins In this study, Li-Al LDH could be activated by modification of acetic acid to improve its adsorption capacity of the specific protein. The characterization of Li-Al LDHs are performed by X-ray Diffraction instrument, Surface Area and Pore Analyzer, Fourier Transform Infrared Spectroscopy, 7Li, 27Al, 13C, and 1H MAS Solid State Spectrometer, Elemental Analyzer, Field Emission Scanning Electron Microscopy and the swelling test. When the Li-Al LDHs are modified by acetic acid, the swellibility has been improved 25% in an aqueous solution. The main composition of the Li-Al LDH lamella is the aluminum hydroxide as the main component. According to the adsorption of Lysozyme, from hen egg white ( Lysozyme), or Bovine Serum Albumin ( BSA ) on pure Li-Al LDH or modified Li-Al LDH. The modified Li-Al LDH can adsorb the most amounts of BSA 383.1 mg/ g, and the minimum amount of Lysozyme 12.8 mg/ g, through the measurement of UV-visible spectrometer. Furthermore, the saturated adsorption of BSA also under the discussion with the modified material, and desorption ability of BSA are studied by the buffer solution of sodium chloride or sodium phosphate. Finally the life cycle of the adsorption-desorption of this material would be understood. Eventually, the BSA and Lysozyme mixture are detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis. There is only Lysozyme in the aqueous solution after adsorption and then BSA can also be desorbed. Thus indicating Layered Double Hydroxides with potential applications for protein purification.