2021
DOI: 10.1016/j.idairyj.2020.104898
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The effect of high-pressure homogenisation on the size of milk fat globules and MFGM composition in sweet buttermilk and milk

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Cited by 27 publications
(15 citation statements)
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“…Increasing the homogenization pressure progressively reduced the size particle, while distributions became narrower, potentially due to the reduction in size of HDL caused by homogenization partially disrupting the granules [ 42 ], as observed for oil-in water emulsions prepared with egg yolk. Similar results were obtained after application of UHPH to milk fat globule membrane (MFGM), which is mainly composed of phospholipids (like yolk granule), in the presence of milk protein [ 43 ]. Simultaneously, increasing the number of passes reduced the sizes of proteins due to the unfolding phenomenon [ 44 ].…”
Section: Discussionsupporting
confidence: 70%
“…Increasing the homogenization pressure progressively reduced the size particle, while distributions became narrower, potentially due to the reduction in size of HDL caused by homogenization partially disrupting the granules [ 42 ], as observed for oil-in water emulsions prepared with egg yolk. Similar results were obtained after application of UHPH to milk fat globule membrane (MFGM), which is mainly composed of phospholipids (like yolk granule), in the presence of milk protein [ 43 ]. Simultaneously, increasing the number of passes reduced the sizes of proteins due to the unfolding phenomenon [ 44 ].…”
Section: Discussionsupporting
confidence: 70%
“…HPP has been shown to alter the size of fat globules and the composition of the MFGM. Pressure can slightly affect the size of fat globules; however, temperature parameters have a greater impact on size; processing milk at temperatures higher than 25 • C yields smaller fat globules, while the opposite is expected when using colder conditions [1,33,34]. Ye et al [34] observed that whole milk subjected to 100-800 MPa promoted β-lactoglobulin (β-lg) association to the MFGM proteins through sulfhydryl disulfide interactions; increased association was promoted at higher pressures; similarly, κ-caseins and α-lactalbumin (α-la) can associate in lower quantities to the MFGM through the same interaction at pressures higher than 500 and 700 MPa, respectively.…”
Section: Lipidsmentioning
confidence: 99%
“…Ye et al [34] observed that whole milk subjected to 100-800 MPa promoted β-lactoglobulin (β-lg) association to the MFGM proteins through sulfhydryl disulfide interactions; increased association was promoted at higher pressures; similarly, κ-caseins and α-lactalbumin (α-la) can associate in lower quantities to the MFGM through the same interaction at pressures higher than 500 and 700 MPa, respectively. These changes and alterations to the MFGM's composition modify its structure, stability, and integrity, as well as the milk's properties, such as its emulsion capacity [33].…”
Section: Lipidsmentioning
confidence: 99%
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