Effect of High Pressure Processing on Properties of Emulsions made with Pure Milk Proteins

Dickinson, Eric; James, Jonathan D.

doi:10.1533/9781845698379.3.152

Cited by 5 publications

(3 citation statements)

References 9 publications

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“…The conformational structure of the β-lactoglobulin gel network appears to share some features in common with a flocculated emulsion system (Doi, 1993). A substantial increase in the viscosity of concentrated β-lactoglobulin-stabilized emulsions following HPT, including the generation of gel-like characteristics, has recently been demonstrated (Dumay et al, 1996;Dickinson and James, 1997).…”

Section: Introductionmentioning

confidence: 97%

Rheology and Flocculation of High-Pressure-Treated β-Lactoglobulin-Stabilized Emulsions: Comparison with Thermal Treatment

Dickinson

James

1998

J. Agric. Food Chem.

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High-pressure treatment (HPT) has been shown to induce significant levels of flocculation in model oil-in-water emulsions stabilized by β-lactoglobulin at neutral pH, as indicated by changes in droplet size distribution and rheological behavior. Light microscopy has also provided additional evidence of extensive droplet flocculation following severe treatment. The proportion of unadsorbed protein greatly influences the extent of flocculation, and this may explain in part the nature of these pressure-induced effects. It has been observed that severe HPT (800 MPa for 60 min) is equivalent to relatively mild thermal treatment (TT) (65 °C for 5 min) in terms of the associated changes in emulsion gel rheology. Since HPT destabilizes these emulsion systems to a much lesser degree than TT, it can be considered to be a gentler processing operation in comparison. Emulsion flocculation is more sensitive to pressure and temperature at pH values closer to the isoelectric point and at higher ionic strength. That is, conditions favoring a loss of electrostatic stability tend to cause an increase in sensitivity toward pressure and temperature, although HPT consistently appears to be a gentler process than TT under all conditions studied. Keywords: High-pressure treatment; thermal treatment; protein functionality; flocculation; rheology; emulsion stability; emulsion gel

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Section: Introductionmentioning

confidence: 97%

Rheology and Flocculation of High-Pressure-Treated β-Lactoglobulin-Stabilized Emulsions: Comparison with Thermal Treatment

Dickinson

James

1998

J. Agric. Food Chem.

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“…High-pressure treatment of emulsion stabilized by low β-lactoglobulin content did not affect the size of droplets or creaminess. A higher level of flocculation occurred after pressure treatment in the presence of a high amount of free (non-absorbed) proteins in the emulsion, due to the unfolding, aggregation, and free proteins acting as a bridge between the dispersed droplets by cross-linking them [94].…”

Section: Impact Of Non-thermal Processing On Proteinsmentioning

confidence: 99%

Bridging the Knowledge Gap for the Impact of Non-Thermal Processing on Proteins and Amino Acids

Esteghlal

Gahruie

Niakousari

et al. 2019

Foods

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Proteins represent one of the major food components that contribute to a wide range of biophysical functions and dictate the nutritional, sensorial, and shelf-life of food products. Different non-thermal processing technologies (e.g., irradiation, ultrasound, cold plasma, pulsed electric field, and high-pressure treatments) can affect the structure of proteins, and thus their solubility as well as their functional properties. The exposure of hydrophobic groups, unfolding followed by aggregation at high non-thermal treatment intensities, and the formation of new bonds have been reported to promote the modification of structural and functional properties of proteins. Several studies reported the reduction of allergenicity of some proteins after the application of non-thermal treatments. The composition and concentration of free amino acids could be changed after non-thermal processing, depending on the processing time and intensity. The present review discusses the effects of different non-thermal treatments on protein properties in detail, and highlights the opportunities and disadvantages of these technologies in relation to protein functionality.

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“…However, HP has a disruptive effect on the tertiary and quaternary structure of the globular proteins (Puppo et al, 2004;Tedford, Smith, & Schaschke, 1999) and non-covalent bonds of protein are altered. Consequently, HP technology adequately controlled can be used to modify functional properties of food components (Dickinson & James, 1998, Montero, Fernández-Díaz, & Gómez-Guillén, 2002.…”

Section: Introductionmentioning

confidence: 99%

β-Conglycinin and glycinin soybean protein emulsions treated by combined temperature–high-pressure treatment

et al. 2011

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Effect of High Pressure Processing on Properties of Emulsions made with Pure Milk Proteins

Cited by 5 publications

References 9 publications

Rheology and Flocculation of High-Pressure-Treated β-Lactoglobulin-Stabilized Emulsions: Comparison with Thermal Treatment

Rheology and Flocculation of High-Pressure-Treated β-Lactoglobulin-Stabilized Emulsions: Comparison with Thermal Treatment

Bridging the Knowledge Gap for the Impact of Non-Thermal Processing on Proteins and Amino Acids

β-Conglycinin and glycinin soybean protein emulsions treated by combined temperature–high-pressure treatment

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