Influence of hydrophobic interfaces and shear on ovalbumin amyloid-like fibril formation in oil-in-water emulsions

Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation

“…Such an aggregation-promoting effect, caused by amyloid fibrils, was also observed in the case of amyloid-beta [ 28 ], as well as alpha-synuclein [ 30 , 31 ]. This could be achieved by either the surface of lysozyme fibrils acting as a catalyst for insulin nucleation events (fibril ends causing a partial misfolding of insulin can be ruled out, as a change in their number did not alter aggregation) or by creating an interface between the solution and its hydrophobic surface (interface-enhanced aggregation [ 39 ]). However, both of these possible mechanisms are only viable at comparatively low LF concentrations, as we observe the appearance of other mechanism-altering effects at a high LF concentration.…”

Nanofibrils of food‐grade proteins: Formation mechanism, delivery systems, and application evaluation

“…Recently, Huyst et al. (2021) prepared O/W emulsions containing OVA nanofibrils via ultra‐turrax homogenization and microfluidization to verify the effect of hydrophobic interfaces and shear on nanofibril formation. They found that the Th T fluorescence of emulsions increased after homogenization and microfluidization treatments, implying the formation of more or larger nanofibril‐like structures, whereas the corresponding serum phases were prepared by ultracentrifugation and were only observed to have a minor change in Th T fluorescence.…”

“…They found that the Th T fluorescence of emulsions increased after homogenization and microfluidization treatments, implying the formation of more or larger nanofibril‐like structures, whereas the corresponding serum phases were prepared by ultracentrifugation and were only observed to have a minor change in Th T fluorescence. In addition, they evaluated links between the specific surface area of oil droplets and protein structures, showing that large hydrophobic interfaces contributed to the formation of larger fibrillar protein structures under microfluidization treatment despite the absence of any heat treatment (Huyst et al., 2021). It was worth noting that the effects of pH values, conformation, and concentration of nanofibrils on the stability of emulsions were usually evaluated based on a complete nanofibril system, which contained denatured proteins and peptides not converted into nanofibrils.…”

Effects of ultrasound pretreatment on functional property, antioxidant activity, and digestibility of soy protein isolate nanofibrils

“…It has been found that protein nanofibrils can improve functional properties such as viscosity [3] , emulsifying properties [4] , foaming properties [5] , antioxidant activity [6] and gelation properties [7] . Many kinds of food proteins can be fibrillated to form protein nanofibrils, such as whey protein [8] , [9] , ovalbumin [10] , rice glutelin [4] , [11] , soy protein [12] , [13] , pea protein [14] , [15] , ovotransferrin [16] , [17] , lysozyme [18] , [19] , etc. Soy protein, as a nutritious, widely available and inexpensive vegetable protein, has aroused great interest in the study of soy protein nanofibrils.…”