Combination of High Hydrostatic Pressure and Ultrafiltration to Generate a New Emulsifying Ingredient from Egg Yolk

Abstract

Egg yolk granule phosvitin (45 kDa) is a phosphoprotein known for its emulsifying properties. Recently, high hydrostatic pressure (HHP) treatment of granule induced the transfer of phosvitin to the soluble plasma fraction. This project evaluated the performance of the ultrafiltration (UF) used to concentrate phosvitin from the plasma fraction to produce a natural emulsifier. Phosvitin was characterized in plasma from a pressure-treated granule (1.73 ± 0.07% w/w) and in its UF retentate (26.00 ± 4.12% w/w). The emulsifying properties of both retentates were evaluated. The emulsion prepared with phosvitin-enriched retentate was more resistant to flocculation and creaming. Confocal laser scanning microscopy showed a network of aggregated protein similar to a gel, which encapsulated oil droplets in emulsions made with UF-retentate of plasma from pressure-treated granule. However, although sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that β-phosvitin is recovered in the cream, it is difficult to attribute the improved emulsifying properties of the UF-retentate of plasma from pressure-treated granules only to phosvitin.

Thoroughly review the recent progresses in improving O/W interfacial properties of proteins through various strategies

“…The effective parameter of HPT varied as species-dependent manner. Some works suggested a ≥ 200 MPa pressure is available in improving interfacial properties, such as in soy protein isolates (400 MPa) ( 53 ), meat protein (200 MPa) ( 54 ), egg yolk protein (400 MPa) ( 55 ) and β-lactoglobulin (600 MPa) ( 29 ). However, in many cases, the increase in interfacial properties can only be observed in moderate pressure.…”

“…One of the mechanisms for HPT in improving protein interfacial activities is by forming a pressure-induced molten globule state in the bulk water phase, which lagged the adsorption period but increased the affinity toward the hydrophobic oil phase ( 29 ). Yang et al ( 1 ) considered the improvement is attributed to depolymerization of interfacial protein through HPT, while in egg yolk granule, the transformation from granule phosvitin to the soluble fraction favored the emulsion properties ( 55 ). To be addressed, the environment also decided the efficiency of HPT.…”

Bioactivities of hen's egg yolk phosvitin and its functional phosphopeptides in food industry and health

“…The hydrophobic terminal structures of phosvitin can be adsorbed at the interface of the oil droplets to stabilize the emulsions. Emulsifying properties of phosvitin can be affected by various factors such as ionic strength, pH, degree of aggregation, freezing/thawing cycles, or heat treatment (Giarratano et al., 2020). In addition, protein concentration, oil volume fraction, emulsion mixing speed, and mixing time can also affect the emulsion.…”

“…Various methods are available for the extraction of phosvitin, which has many functional properties, mainly metal‐binding properties and resistance to proteolytic enzymes. Because these methods are costly and time‐consuming, as well as they cannot be adapted to the food industry and are not sustainable, different methods are tried for the extraction of phosvitin (Giarratano et al., 2020). Enzymatic hydrolysis is one of these methods, which can be broken down into the peptides of phosvitin in this way.…”

Impact of Ultra-High Pressure Homogenization on the Structural Properties of Egg Yolk Granule

“…After centrifugation of the isostatically pressured granule, the recovered insoluble fraction was enriched in folic acid and phosvitin. Consequently, the use of high pressure shows great potential to generate new ingredients with interesting nutritional and functional properties for many industrial applications such as use as a low-cholesterol emulsifying agent in mayonnaise [ 11 , 12 , 13 , 14 , 15 ].…”