The adsorption characteristics of 2D fibril and 3D hydrogel aggregates at the O/W interface combining molecular dynamics simulation

Spread Layers of Lysozyme Microgel at Liquid Surface

“…The application of protein aggregates in food, pharmaceutical, and cosmetic branches of industry, in particular to create foams and emulsions of high stability, resulted in recent years in numerous publications on surface properties of aggregate dispersions [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 ], mainly of dispersions of β-lactoglobulin (BLG) [ 2 , 5 , 12 , 13 , 14 , 15 , 21 , 27 , 30 , 32 , 33 , 34 , 37 ] or whey protein [ 1 , 4 , 19 ,…”

Aggregate Size Modulates the Oil/Water Interfacial Behavior of Myofibrillar Proteins: Toward the Thicker Interface Film and Disulfide Bond

“…Overall, the above results corroborated our initial hypothesis that once large MP aggregates were adsorbed into the O/W interface, thicker and more viscoelastic interfacial films would form to effectively resist surfactant-induced competitive displacement, inhibiting the emulsion destabilization. To the best of our knowledge, this is the first study to focus on the influence of the aggregate size on the interfacial properties of MP from a multiscale evaluation containing macroscopic, mesoscopic, and microcosmic perspectives, which was neglected in previous studies to some extent. ,,, A highlight of the current work is that we found the MP-aggregate size was capable of the oriented manipulation of interfacial film formation. And we also confirmed that S–S linkage was the primary cross-link to stabilize the interfacial film .…”

“…34 The interfacial protein concentration corresponds to the thickness of the interfacial protein film, that is to say, the higher the Γ in the adsorption layer, the thicker the interfacial film. 9,51,73 As listed in Table 1, the Γ for aggregate groups was significantly higher than the untreated group, indicating a stronger interfacial protein load consistent with the result of Cui et al 74 In aggregate groups, LA (13.53 mg/m 2 ) exhibited higher Γ (P < 0.05) than SA (11.16 mg/m 2 ), implying that the interfacial layer formed by MP aggregates was thicker with the increase of the aggregate size, which is in accordance with the result described earlier (section Interfacial Layer Thickness).…”

“…The destabilization of protein-stabilized emulsion would take place via various physicochemical mechanisms containing creaming, flocculation, coalescence, and Ostwald ripening . Several physicochemical approaches (e.g., ultrasound and pH-shifting) to reverse the negative implications of emulsion destabilization have been identified. − In these cases, the formation of protein aggregates is inevitable due to the high self-aggregating nature of proteins. − The properties of aggregated protein-involved emulsions were commonly influenced by the morphology and size of the aggregate, the charge screening, and the ratio of denatured native-like monomers, − one of the most important of which is the aggregate size.…”

A Perspective on Methods to Computationally Design the Morphology of Aerogels

“…However, the premise is promising given that such molecular dynamics-based simulations have addressed important issues in describing hydrogels. [22][23][24][25][26] With respect to aerogels, this is an important subject that needs to be addressed, however, more elaboration at this point may drift the reader of this article off-topic. To this end, molecular dynamics-based models will not be considered in this article, but a special focus will be on mesoscopic models and their applicability to design the 3D morphology of aerogels.…”