Formation of Natural Egg Yolk Granule Stabilized Pickering High Internal Phase Emulsions by Means of NaCl Ionic Strength and pH Change

Pickering high internal phase emulsions (HIPEs) are gel-like concentrated emulsions that have the potential to be an alternative to partially hydrogenated oil (PHO). In this study, egg yolk granules (EYGs), natural complexes of protein and lipid isolated from egg yolk, were used as an emulsifier to prepare Pickering HIPEs. Gel-like HIPEs with an oil phase volume fraction of 85% and with an emulsifier concentration of only 0.5% could be prepared by using EYGs as an emulsifier. The EYGs were able to form stable HIPEs at NaCl ionic strengths over 0.2 M and at pH over 5.0 with NaCl ionic strength of 0.3 M. The EYGs, which could stabilize HIPEs, were easily to adsorb and cover the oil-water interface to form emulsion droplets with small particle size. In addition, interacting EYGs in the aqueous phase formed a continuous network structure, and the oil droplets packed closely, exhibiting high elasticity and shear thinning behavior. Furthermore, the formed HIPEs had suitable storage stability with no significant changes in appearance and microstructure after storage for 60 days. This work can transform traditional oils from liquid-like to solid-like by using EYGs to enrich food processing diversity and improve the storage stability of oils while reducing the intake of PHO and providing a healthier diet for consumers.

Building programmable multicompartment artificial cells incorporating remotely activated protein channels using microfluidics and acoustic levitation

Intracellular compartments are functional units that support the metabolic processes within living cells, through spatiotemporal regulation of chemical reactions and biological processes. Consequently, as a step forward in the bottom-up creation of artificial cells, building analogous intracellular architectures is essential for the expansion of cell-mimicking functionality. Herein, we report the development of a droplet laboratory platform to engineer customised complex emulsion droplets as a multicompartment artificial cell chassis, using multiphase microfluidics and acoustic levitation. Such levitated constructs provide free-standing, dynamic, definable droplet networks for the encapsulation and organisation of chemical species. Equally, they can be remotely operated with pneumatic, heating, and magnetic elements for post-processing, including the incorporation of membrane proteins; alpha-hemolysin; and large-conductance mechanosensitive channel (MscL) and their activation. The assembly of droplet networks is three-dimensionally patterned with fluidic inputs configurations determining droplet contents and connectivity. Whilst acoustic manipulation can be harnessed to reconfigure the droplet network in situ. In addition, a mechanosensitive channel, MscL, can be repeatedly activated and deactivated in the levitated artificial cell by the application of acoustic and magnetic fields to modulate membrane tension on demand. This offers possibilities beyond one-time chemically mediated activation to provide repeated, non-contact control of membrane protein function. Collectively, this will expand our capability to program and operate increasingly sophisticated artificial cells as life-like materials.

Microfluidics as a tool to assess and induce emulsion destabilization

Microfluidic technology enables a judicious control of the process parameters on a small length-scale, which in turn allows speeding up the destabilization of emulsion droplets interface in microfluidic devices. In...

Mechanisms of Change in Emulsifying Capacity Induced by Protein Denaturation and Aggregation in Quick-Frozen Pork Patties with Different Fat Levels and Freeze–Thaw Cycles

Herein, we discuss changes in the emulsifying properties of myofibrillar protein (MP) because of protein denaturation and aggregation from quick-frozen pork patties with multiple fat levels and freeze–thaw (F–T) cycles. Protein denaturation and aggregation were confirmed by the significantly increased surface hydrophobicity, turbidity, and particle size, as well as the significantly decreased solubility and absolute zeta potential, of MPs with increases in fat levels and F–T cycles (p < 0.05). After multiple F–T cycles, the emulsifying activity and emulsion stability indices of all samples were significantly reduced (p < 0.05). The emulsion droplets of MP increased in size, and their distributions were dense and irregular. The results demonstrated that protein denaturation and aggregation due to multiple F–T cycles and fat levels changed the distribution of surface chemical groups and particle sizes of protein, thus affecting the emulsifying properties.