球狀蛋白，是一種廣泛應用於科學上且扮演著關鍵作用的蛋白質，其物理與化學性質在過去的幾十年內也被大量的探討與研究。然而迄今為止，球狀蛋白質在氣-液界面的吸附膜之物化特性尚不甚清楚。本論文擬探討牛血清白蛋白質 (Bovine Serum Albumin – BSA)水溶液之吸附行為，並藉懸垂氣泡影像數位化測量儀來量測BSA吸附薄膜的擴張模量。
本研究量測BSA分子吸附到乾淨的氣-液界面之動態表面張力和氣泡表面積，其張力需2~5天才達平衡。於BSA吸附後期階段，表面張力可保持近乎恆定達數十小時。因此，可以合理地認定此張力是BSA水溶液的平衡表面張力。在0.052 – 15 (10-10 mol/cm3) 濃度範圍中，其平衡張力維持在51.50.3 mN/m 。
本研究亦嘗試探討BSA水溶液在氣-液界面的吸附機制。將初始時段之動態表面張力數據與擴散(或混合)控制吸附的模型進行最佳比對，結果顯示：BSA水溶液吸附到氣-液界面呈混合控制機制。本研究亦探討如何估算(在不知平衡表面張力數據的情況下)最大表面濃度 () 和吸附的 BSA 分子之分子間相互作用 (K) 的新方法：將氣泡表面擴張期間 (在BSA吸附後期階段) 之動態表面張力與表面狀態方程式進行最佳比對。比對結果可粗估獲知BSA分子的  與K 的值。
於BSA水溶液吸附程序的後期階段，系統檢測到有諸多微小和低頻的界面擾動。蓋因於環境溫度的細微變化 (1 C)。藉由分析這些擾動所引起的張力和表面積之變化，可用來評估表面擴張速率 [d(lnA)/dt] 和表面張力變化速率 (dγ/dt)；對 dγ/dt 與 d(lnA)/dt 作圖，數據呈線性變化，其斜率可粗估獲得其擴張模量：E = dγ/d(lnA)。在BSA濃度為0.05210-10和1510-10 mol/cm3時，BSA薄膜的擴張模量分別為43和30 mN/m。此實驗提供了在氣-液界面受到微小和低頻〔1 – 2%振幅， ~10-4 Hz頻率，低於傳統~10-2 Hz〕的界面擾動情況下，測量擴張模量的可行性。

The physicochemical properties of globular protein have been extensively studied over the last few decades as they play a pivotal role in numerous scientific applications. Despite notable advancements, the adsorption of globular proteins onto the air-water interface is not well understood to date. Hence, this dissertation majorly focuses on investigating the adsorption of globular protein – bovine serum albumin (BSA) and evaluating the dilatational modulus of BSA films by pendant bubble tensiometry.
In this study, the surface tension (ST) relaxations, due to the adsorption of BSA molecules onto a clean air-water interface, were measured for 2 – 5 days. The ST remained nearly constant for several tens of hours at the latter stage of BSA adsorption. Therefore, it is reasonable to assume that these near-constant values of ST are the equilibrium ST of BSA solutions. The equilibrium ST kept at 51.50.3 mN/m for a wide range of concentration [0.052 – 15 (10-10 mol/cm3)].
The adsorption mechanism of BSA onto the air-water interface was additionally examined. The initial regions of the dynamic ST data were best-fitted with the model predictions for diffusion-controlled or mixed diffusive-kinetic controlled adsorption processes. The results of these fitting indicated that the adsorption of BSA onto the air-water interface was likely mixed-controlled. Moreover, a new approach for estimating the maximum surface concentration () and the intermolecular interaction amongst the adsorbed BSA molecules (K) was trialed. The relaxation of ST during a surface expansion, performed at the latter stage of BSA adsorption, was best fitted with the surface equation of state. A reasonably good fitting revealed that the values of  and K for BSA could be estimated without requiring the equilibrium ST data.
At the latter stage of the BSA adsorption process, numerous minute and low-frequency interfacial perturbances (due to minor variations in ambient temperature, 1 C) were detected. These perturbances were analyzed to evaluate the surface dilatational rate [d(lnA)/dt] and rate of ST change (dγ/dt). The dilatational modulus [E = dγ/d(lnA)] was then obtained from the slope of the linear best-fit in the plot of dγ/dt vs d(lnA)/dt. The dilatational modulus of BSA films at a concentration of 0.05210-10 and 1510-10 mol/cm3 was found to be 43 and 30 mN/m, respectively. These results verified the feasibility of obtaining the dilatational modulus with extremely low frequency surface perturbances.

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