Application of pressure homogenization on whole human milk pasteurized by high hydrostatic pressure: Effect on protein aggregates in milk fat globule membrane and skim milk phases.

This study explored the impact of homogenization (at pressures of 16, 30, and 45 MPa) on both raw and high hydrostatic pressure (HHP)-treated human milk (HM). It focused on protein compositions and binding forces of soluble and insoluble fractions for both milk fat globule membrane (MFGM) and skim milk. Mild homogenization of HHP-treated milk increased lactoferrin (LF) levels in the insoluble fractions of both MFGM and skim milk, due to insoluble aggregation through hydrophobic interactions. Intense homogenization of HHP-treated milk decreased the LF level in the MFGM fractions due to the LF desorption from the MFGM, which increased LF level in the insoluble skim milk fraction. Homogenized-HHP treated milk showed noticeably higher casein (CN) level at the MFGM compared to homogenized-raw milk, attributed to HHP effect on CN micelles. Overall, the combined use of HHP and shear-homogenization should be avoided as it increased the biological proteins in insoluble fractions.

Characterization of protein aggregates in cream and skimmed human milk after heat and high-pressure pasteurization treatments.

Preservation processes applied to ensure microbial safety of human milk (HM) can modify the native structure of proteins and their bioactivities. Consequently, this study evaluated the effect of pasteurization methods (Holder pasteurization, high-temperature short-time (HTST), and high hydrostatic pressure (HHP)) of whole human milk (HM) on protein aggregates in skim milk and cream fractions. For heat-treated whole milk, insoluble protein aggregates at milk fat globule membrane (MFGM) were formed by disulfide and non-covalent bonds, but insoluble skim milk protein aggregates were only stabilized by non-covalent interactions. Contrary to heat treatment, the insolubilization of main proteins at the MFGM of HHP-treated HM was only through non-covalent interactions rather than disulfide bonds. Moreover, only heat treatment induced the insoluble aggregation of ⍺-lactalbumin. Overall, compared to heat treatment, HHP produced a milder effect on protein aggregation, validating the use of this process to better preserve the native state of HM bioactive proteins.

Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review.

High hydrostatic pressure (HHP) treatment induces structural changes in bovine milk proteins depending on factors such as the temperature, pH, concentration, decompression rate, cycling, composition of the medium and pressure level and duration. An in-depth understanding of the impact of these factors is important for controlling HHP-induced modification of milk proteins and the interactions within or between them, which can be applied to prevent undesired aggregation, gelation, and precipitation during HHP processing or to obtain specific milk protein modifications to attain specific protein properties. In this regard, understanding the influences of these factors can provide insight into the modulation and optimization of HHP conditions to attain specific milk protein structures. In recent years, there has been a great research attention on HHP-induced changes in milk proteins influenced by factors such as pH, temperature, concentration, cycling, decompression condition, and medium composition. Hence, to provide insight into how these factors control milk protein structures under HHP treatment and to understand if their effects depend on HHP parameters and environmental conditions, this review discusses recent findings on how various factors (pH, temperature, cycling, decompression rate, medium composition, and concentration) affect HHP-induced bovine milk protein modification. Practical Application: The information provided in this review will be very useful to anticipate the challenges related to the formulation and development of pressure-treated milk and dairy products.

Effect of processing on aggregation mechanism of egg white proteins.

Egg white proteins (EWPs) are important components of many food products. To obtain optimal functionality, EWP aggregation needs to be controlled. Different treatments can lead to the formation of aggregates in diverse ways, depending on the parameters of the treatments. Recent articles on the effects of processing (heat treatment, alkali treatment, pulsed electric field, high pressure, ultraviolet irradiation, and high intensity ultrasound) on the aggregation of EWPs are reviewed. The relationships between the processing parameters and the aggregation mechanisms are discussed. The information may be helpful in controlling the aggregation mechanisms during the processing.