Globular proteins have been the subject of extensive scientific investigations to date. Despite significant progress, essential aspects concerning the surface tension (ST) and dilational rheology of globular proteins are still unclear; including the influence of buffer concentration (Cbuffer) on ST, desorption from an air-water interface, and the effect of adsorption process on dilational modulus (E) measurement. Consequently, this dissertation aims to address these knowledge gaps.
The influence of buffer concentration (standard phosphate) on the dynamic/equilibrium ST of bovine serum albumin (BSA) solutions was examined. A pendant bubble tensiometer was utilized for measuring the ST relaxation at Cbuffer = 0 – 300 mM. The data showed: (i) a preliminary increase in Cbuffer (< 0.3 mM) corresponded to a slower ST relaxation and an elevation in the equilibrium ST; and (ii) at Cbuffer > 0.3 mM, the ST relaxed faster while the equilibrium ST progressively declined. Furthermore, the dynamic ST always relaxed the slowest at Cbuffer = 0.3 mM, despite a near 8-time increase in CBSA [2.0 to 15 (10-10 mol/cm3)].
The equilibrium ST of globular protein solutions was often reported to decrease at increasing bulk concentration. However, a recent study revealed it to be constant for purely aqueous BSA solutions over a broad concentration range, raising concerns about it being an anomaly. Hence, the equilibrium ST of lysozyme (LYS) and BSA in an aqueous phosphate buffer were evaluated. The data showed that regardless of the protein/solvent, the equilibrium ST of BSA and LYS were constant (~54.0 and ~50.0 mN/m, respectively) at C = 0.052 – 500 (10-10 mol/cm3); thereby confirming the constant equilibrium ST behavior to not be an anomaly.
Conflicting reports exist in the literature concerning the desorption of proteins from an air-water interface, the prevailing idea being that globular proteins cannot desorb. Additional tests were conducted for aqueous BSA, HSA, and LYS solutions: the pendant bubble being subjected to a forced, rapid compression at a latter adsorption stage. Post compression, the ST fell to a distinct minimum, far below its equilibrium ST; wherein the adsorbed protein film was likely overcrowded. The ST eventually returned to nearly the same equilibrium ST value, thereby demonstrating that BSA, HSA, and LYS can desorb from the air-water interface into the bulk phase.
The variation of E for an adsorbed BSA film was monitored during the adsorption process (from a clean air-water interface to a saturated state). The data showed that E decreased sharply to a minimum at the early stage of BSA adsorption, rose, and oscillated for a while before reaching an E corresponding to a saturated BSA film. The time needed for the adsorbed film to reach its saturated state was found to be ~35 hours; which was much longer than the time required to reach the equilibrium ST, as well as the lifetime of an adsorbed film reported in the literature [0.05 – 24 hours].

Globular proteins have been the subject of extensive scientific investigations to date. Despite significant progress, essential aspects concerning the surface tension (ST) and dilational rheology of globular proteins are still unclear; including the influence of buffer concentration (Cbuffer) on ST, desorption from an air-water interface, and the effect of adsorption process on dilational modulus (E) measurement. Consequently, this dissertation aims to address these knowledge gaps.
The influence of buffer concentration (standard phosphate) on the dynamic/equilibrium ST of bovine serum albumin (BSA) solutions was examined. A pendant bubble tensiometer was utilized for measuring the ST relaxation at Cbuffer = 0 – 300 mM. The data showed: (i) a preliminary increase in Cbuffer (< 0.3 mM) corresponded to a slower ST relaxation and an elevation in the equilibrium ST; and (ii) at Cbuffer > 0.3 mM, the ST relaxed faster while the equilibrium ST progressively declined. Furthermore, the dynamic ST always relaxed the slowest at Cbuffer = 0.3 mM, despite a near 8-time increase in CBSA [2.0 to 15 (10-10 mol/cm3)].
The equilibrium ST of globular protein solutions was often reported to decrease at increasing bulk concentration. However, a recent study revealed it to be constant for purely aqueous BSA solutions over a broad concentration range, raising concerns about it being an anomaly. Hence, the equilibrium ST of lysozyme (LYS) and BSA in an aqueous phosphate buffer were evaluated. The data showed that regardless of the protein/solvent, the equilibrium ST of BSA and LYS were constant (~54.0 and ~50.0 mN/m, respectively) at C = 0.052 – 500 (10-10 mol/cm3); thereby confirming the constant equilibrium ST behavior to not be an anomaly.
Conflicting reports exist in the literature concerning the desorption of proteins from an air-water interface, the prevailing idea being that globular proteins cannot desorb. Additional tests were conducted for aqueous BSA, HSA, and LYS solutions: the pendant bubble being subjected to a forced, rapid compression at a latter adsorption stage. Post compression, the ST fell to a distinct minimum, far below its equilibrium ST; wherein the adsorbed protein film was likely overcrowded. The ST eventually returned to nearly the same equilibrium ST value, thereby demonstrating that BSA, HSA, and LYS can desorb from the air-water interface into the bulk phase.
The variation of E for an adsorbed BSA film was monitored during the adsorption process (from a clean air-water interface to a saturated state). The data showed that E decreased sharply to a minimum at the early stage of BSA adsorption, rose, and oscillated for a while before reaching an E corresponding to a saturated BSA film. The time needed for the adsorbed film to reach its saturated state was found to be ~35 hours; which was much longer than the time required to reach the equilibrium ST, as well as the lifetime of an adsorbed film reported in the literature [0.05 – 24 hours].

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