Advances in CO2-switchable surfactants towards the fabrication and application of responsive colloids.

CO2-switchable surfactants have selective surface-activity, which can be activated or deactivated either by adding or removing CO2 from the solution. This feature enables us to use them in the fabrication of responsive colloids, a group of dispersed systems that can be controlled by changing the environmental conditions. In chemical processes, including extraction, reaction, or heterogeneous catalysis, colloids are required in some specific steps of the processes, in which maximum contact area between immiscible phases or reactants is desired. Afterward, the colloids must be broken for the postprocessing of products, solvents, and agents, which can be facilitated by using CO2-switchable surfactants in surfactant-stabilized colloids. These surfactants are mainly cationic and can be activated by the protonation of a nitrogen-containing group upon sparging CO2 gas. Also, CO2-switchable superamphiphiles can be formed by non-covalent bonding between components at least one of which is CO2-switchable. So far, CO2-switchable surfactants have been used in CO2-switchable spherical and wormlike micelles, vesicles, emulsions, foams, and Pickering emulsions. Here, we review the fabrication procedure, chemical structure, switching scheme, stability, environmental conditions, and design philosophy of such responsive colloids. Their fields of application are wide, including emulsion polymerization, catalysis, soil washing, drug delivery, extraction, viscosity control, and oil transportation. We also emphasize their application for the CO2-assisted enhanced oil recovery (EOR) process as a promising approach for carbon capture, utilization, and storage to combat climate change.

Experimental techniques to study protein-surfactant interactions: New insights into competitive adsorptions via drop subphase and interface exchange.

Protein surfactant (PS) interactions is an essential topic for many fundamental and technological applications such as life science, nanobiotechnology processes, food industry, biodiesel production and drug delivery systems. Several experimental techniques and data analysis approaches have been developed to characterize PS interactions in bulk and at interfaces. However, to evaluate the mechanisms and the level of interactions quantitatively, e.g., PS ratio in complexes, their stability in bulk, and reversibility of their interfacial adsorption, new experimental techniques and protocols are still needed, especially with relevance for in-situ biological conditions. The available standard techniques can provide us with the basic understanding of interactions mainly under static conditions and far from physiological criteria. However, detailed measurements at complex interfaces can be formidable due to the sophisticated tools required to carefully probe nanometric phenomena at interfaces without disturbing the adsorbed layer. Tensiometry-based techniques such as drop profile analysis tensiometry (PAT) have been among the most powerful methods for characterizing protein's and surfactant's adsorption layers at interfaces via measuring equilibrium and dynamic interfacial tension and dilational rheology analysis. PAT provides us with insightful data such as kinetics and isotherms of adsorption and related surface activity parameters. However, the data analysis and interpretation can be challenging for mixed protein-surfactant solutions via standard PAT experimental protocols. The combination of a coaxial double capillary (micro flow exchange system) with drop profile analysis tensiometry (CDC-PAT) is a promising tool to provide valuable results under different competitive adsorption/desorption conditions via novel experimental protocols. CDC-PAT provides unique experimental protocols to exchange the droplet subphase in a continuous dynamic mode during the in-situ analysis of the corresponding interfacial adsorbed layer. The contribution of diffusion/convection mechanisms on the kinetics of the adsorption/desorption processes can also be investigated using CDC-PAT. Here, firstly, we review the commonly available techniques for characterizing protein-surfactant interactions in the bulk phase and at interfaces. Secondly, we give an overview for applications of the coaxial double capillary PAT setup for investigations of mixed protein-surfactant adsorbed layers and address recently developed protocols and analysis procedures. Exploring the competitive sequential adsorption of proteins and surfactants and the reversibility of pre-adsorbed layers via the subphase exchange are the particular experiments we can perform using CDC-PAT. Also the sequential and simultaneous competitive adsorption/desorption processes of some ionic and nonionic surfactants (SDS, CTAB, DTAB, and Triton) and proteins (bovine serum albumin (BSA), lysozyme, and lipase) using CDC-PAT are discussed. Last but not least, the fabrication of micro-nanocomposite layers and membranes are additional applications of CDC-PAT discussed in this work.

Enzymatic Hydrolysis of Triglycerides at the Water-Oil Interface Studied via Interfacial Rheology Analysis of Lipase Adsorption Layers.

The enzymatic hydrolysis of sunflower oil occurs at the water-oil interface. Therefore, the characterization of dynamic interfacial phenomena is essential for understanding the related mechanisms for process optimizations. Most of the available studies for this purpose deal with averaged interfacial properties determined via reaction kinetics and dynamic surface tension measurements. In addition to the classical approach for dynamic surface tension measurements, here, the evolution of the dilational viscoelasticity of the lipase adsorbed layer at the water-oil interface is characterized using profile analysis tensiometry. It is observed that lipase exhibits nonlinear dilational rheology depending on the concentration and age of the adsorbed layer. For reactive water-oil interfaces, the response of the interfacial tension to the sinusoidal area perturbations becomes more asymmetric with time. Surface-active products of the enzymatic hydrolysis of triglycerides render the interface less elastic during compression compared to the expansion path. The lipolysis products can facilitate desorption upon compression while inhibiting adsorption upon expansion of the interface. Lissajous plots provide an insight into how the hysteresis effect leads to different interfacial tensions along the expansion and compression routes. Also, the droplet shape increasingly deviates from a Laplacian shape, demonstrating an irreversible film formation during aging and ongoing hydrolysis reaction, which supports our findings via interfacial elasticity analysis.

Dynamics of Competitive Adsorption of Lipase and Ionic Surfactants at the Water-Air Interface.

Lipase is one of the most important enzymes playing a key role in many biological and chemical processes, in particular for fat hydrolysis in living systems and technological applications such as food production, medicine, and biodiesel production. As lipase is soluble in water, the major hydrolysis process occurs at the water-oil interface, where lipase can get in contact with the oil. To provide optimum conditions, the emulsification of the oil is essential to provide a large interfacial area which is generally done by adding surfactants. However, the presence of surfactants can influence the lipase activity and also cause competitive adsorption, resulting in a removal of lipase from the interface or its conformational changes in the solution bulk. Here we have studied the dynamics of competitive adsorption and interfacial elasticity of mixed solutions containing lipase and the anionic surfactant sodium dodecyl sulfate (SDS) or the cationic surfactant cetyltrimethylammonium bromide (CTAB), respectively, at the water-air interface. The experiments were performed with a special coaxial double capillary setup for drop bulk-interface exchange developed for the drop profile analysis tensiometer PAT with two protocols: sequential and simultaneous adsorption of single components and mixed systems. The results in terms of dynamic surface tension and dilational viscoelasticity illustrate fast and complete desorption of a preadsorbed CTAB and SDS layers via subphase exchange with a buffer solution. In contrast, the preadsorbed lipase layer cannot be removed either by SDS or CTAB from the interface during drop bulk exchange with a buffer solution due to the unfolding process and conformation evolution of the protein molecules at the interface. In the opposite case, lipase can remove preadsorbed SDS and CTAB. The dynamic surface tension and viscoelasticity data measured before and after subphase exchange show joint adsorption of lipase and CTAB in the form of complexes, while SDS is adsorbed in competition with lipase. The results are in good correlation with the determined surface charges of the lipase gained by computational simulations which show a dominant negatively charged surface for lipase that can interact with the cationic CTAB while partial positively charged regions are observed for the interaction with the anionic SDS.