本論文係有關於磁性奈米載體在生物觸媒與生化分離上之應用研究。前者主要將酵母菌類醇脫氫酵素(YADH)固定化在四氧化三鐵(Fe3O4)磁性奈米載體上，探討製備變因、產品特性、及其在水相系統和逆微胞系統中之操作性能；此外，也探討YADH在混合逆微胞系統中的穩定性與活性。後者主要將聚丙烯酸(PAA)共價鍵結在Fe3O4磁性奈米載體上，作為一種新型磁性奈米吸附劑，探討製備變因、產品特性、及其在水相溶菌酶吸附分離上的應用。

　　關於YADH在混合逆微胞系統中之穩定性與活性研究，係將非離子型界面活性劑(Brij30)加入含陰離子型界面活性劑(AOT)的逆微胞系統中，探討其對YADH穩定性與活性的影響。以動態光散射儀(DLS)量測得知，混合逆微胞的水力直徑分佈和平均水力直徑會隨著水與界面活性劑的莫耳比(Wo值)及Brij30濃度的不同而不同，並且影響YADH的活性和穩定性。當混合逆微胞的電荷密度、結合水份、大小、及因AOT和Brij30間之親水性引力所捕捉的水份等變因減低時，YADH的穩定性隨之增加。至於YADH在混合逆微胞中的活性，也同時受到酵素和界面活性劑間的靜電引力和疏水性引力、逆微胞大小及水份結合程度所影響。除了逆微胞有一最適當之水力直徑外，其它因素的降低，將有助於YADH活性的提升。

　　關於YADH固定化在Fe3O4磁性奈米載體上之研究，首先以化學共沉法製備出Fe3O4磁性奈米粒子，然後將YADH利用carbodiimide活化的方式直接固定化在磁性奈米粒子上，並再探討其操作在水相和逆微胞系統中的操作性能。由穿透式電子顯微鏡(TEM)、X射線繞射儀(XRD)和超導量干涉磁量儀(SQUID磁量儀)分析得知，磁性奈米粒子在YADH固定化後，其大小、結構和超順磁性並無明顯改變。傅立葉轉換紅外線光譜儀(FTIR)分析可確認YADH確實已固定化在磁性奈米粒子上，並推測其一可能的反應機構。固定化YADH在水相系統中擁有62 %的殘餘活性及良好的穩定性，相關的動力行為在本研究中皆有探討。將固定化YADH操作在water/AOT/isooctane的逆微胞系統中，發現NADH和水會分佈在磁性粒子表面上和逆微胞的水池中。隨著Wo值的增加，磁性粒子表面上的水膜厚度亦隨之增加。在固定的NADH莫耳數下，NADH在逆微胞水池中的濃度不受Wo值影響。除了水量外，在相似條件下，固定化YADH在逆微胞系統中的殘餘活性為其在水相系統中的40 %，且固定化YADH在逆微胞系統中的穩定性極佳。另外，固定化YADH在逆微胞系統中的動力行為在本研究中也有探討。

　　關於磁性奈米吸附劑之製備與應用，首先以化學共沉法製備出Fe3O4磁性奈米粒子，然後將PAA藉carbodiimide活化直接共價鍵結在磁性奈米粒子上，形成具有離子交換功能之磁性奈米載體，並再探討其在水相溶菌酶吸附分離上的應用。由TEM、XRD和SQUID磁量儀分析得知，磁性奈米粒子在共價鍵結PAA後，其大小、結構和超順磁性並無明顯改變。由FTIR、熱重分析儀(TGA)、熱差分析儀(DTA)和化學分析電子光譜儀(XPS)分析可確認PAA已共價鍵結在磁性奈米粒子上。本研究所得的磁性奈米吸附劑，其離子交換容量為1.64 meq/g，遠較一般商業化的吸附劑為高。由於磁性奈米吸附劑具有高的比面積且無孔內擴散阻力，故磁性奈米吸附劑能在1分鐘內就將溶菌酶完全吸附或脫附，且經吸附脫附程序後，其殘餘活性仍達95 %。至於水相溶菌酶在磁性奈米吸附劑上的吸附，可以Langmuir恆溫吸附模式描述。

　　This dissertation concerns the applications of nano-sized magnetic carries in biocatalysis and bioseparation. In the former, yeast alcohol dehydrogenase (YADH) was immobilized on Fe3O4 magnetic nanoparticles. The preparation conditions, product properties, and the performances in both the water and microemulsion systems were investigated. In addition, the stability and activity of YADH in the mixed reverse micelles was also studied. In the latter, polyacrylic acid (PAA) was covalently bound onto Fe3O4 magnetic nanoparticles to be a novel nano-adsorbent. The preparation conditions, product properties, and the application in the adsorption of lysozyme in aqueous solution were investigated.

　　The stability and activity of YADH in the mixed reverse micelles were studied by adding Brij30 to the AOT reverse micelles. By the investigation on the hydrodynamic diameter of mixed reverse micelles and its distribution via dynamic light scattering, it was suggested that the structure of mixed reverse micelles and the stability of YADH were determined by four important factors, including the surface charge density, bound water, reverse micellar size, and the entrapment of water by hydrophilic-hydrophilic interaction of AOT and Brij30. The effects of these four factors on the stability of YADH at various Wo values and Brij30 concentration have been discussed. When they were decreased, the stability of YADH might be improved. In addition, it was found that the activity of YADH in AOT/Brij30 mixed reverse micelles might be enhanced at appropriate Brij30 concentrations and ω0 values. According to the hydrodynamic diameter of mixed reverse micelles and its distribution, three main factors were suggested. They were the hydrophobic and electrostatic interactions between enzyme and surfactants, the reverse micellar size, and the bound degree of water molecules. An optimal reverse micellar size and the decreases of other two factors would lead to the enhancement of enzyme activity.

　　YADH was covalently bound onto Fe3O4 magnetic nanoparticles via carbodiimide activation. The magnetic nanoparticles with a mean diameter of 10.6 nm were prepared by co-precipitating Fe2+ and Fe3+ ions in an ammonia solution and treating under hydrothermal conditions. From the analyses of Transmission electron microscopy (TEM), X-ray diffraction (XRD) and magnetism, the magnetic nanoparticles showed no changes in size, structure and superparamagnetic characteristics after binding YADH. The analysis of Fourier transform infrared (FTIR) spectroscopy confirmed the binding of YADH to magnetic nanoparticles and suggested a possible binding mechanism. The bound YADH retained 62% of its original activity and exhibited improved stability. The kinetic behavior of bound YADH was also determined in aqueous solution. In addition, the performance of YADH-bound magnetic nanoparticles in the NADH-containing water-in-oil microemulsions of water/AOT/isooctane was examined. Both water and NADH were present in the aqueous phase of microemulsion solution and on particle surface. The thickness of aqueous film on particle surface increased with increasing the Wo value. At a constant NADH amount, the concentration of NADH in the aqueous phase of microemulsion solution was not significantly affected by the Wo value. The specific activity of bound YADH in the microemulsion system was 40% of that in aqueous solution. The bound YADH showed excellent storage stability and good thermal stability in the microemulsion system. The kinetic behavior of bound YADH in the microemulsion system was also determined.

　　PAA was covalently bound onto Fe3O4 magnetic nanoparticles via carbodiimide activation. The magnetic nanoparticles with a mean diameter of 13.2 nm were prepared by co-precipitating Fe2+ and Fe3+ ions in an ammonia solution and treating under hydrothermal conditions. From the analyses of TEM, XRD and magnetism, the magnetic nanoparticles showed no change in size, structure and superparamagnetic characteristics after binding PAA. The analyses of FTIR, thermogravimetric analysis (TGA), differential thermal analysis (DTA) and X-ray photoelectron spectroscopy (XPS) confirmed the binding of PAA to magnetic nanoparticles and suggested the binding mechanism of PAA. The ionic exchange capacity of the resultant magnetic nano-adsorbents was estimated to be 1.64 meq/g, much higher than those of the commercial ionic exchange resins. When the magnetic nano-adsorbents were used for the recovery of lysozyme, it was found that the adsorption/desotption of lysozyme was achievable within 1 min due to the absence of pore-diffusion resistance and the specific activity of recovered lysozyme retained 95% of its original activity. In addition, the adsorption behavior followed the Langmuir adsorption isotherm.

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