Casein micelle dissociation in skim milk during high-pressure treatment: Effects of pressure, pH, and temperature

Effects of high pressure (HP) on average casein micelle size and denaturation of α-lactalbumin (α-la) and β-lactoglobulin (β-lg) in raw skim bovine milk were studied over a range of conditions. Micelle size was not influenced by treatment at pressures <200 MPa, but treatment at 250 MPa increased micelle size by ∼25%, while treatment at [ges ]300 MPa irreversibly reduced it to ∼50% of that in untreated milk. The increase in micelle size after treatment at 250 MPa was greater with increasing treatment time and temperature and milk pH. Treatment times [ges ]2 min at 400 MPa resulted in similar levels of micelle disruption, but increasing milk pH to 7·0 partially stabilised micelles against HP-induced disruption. Denaturation of α-la did not occur [les ]400 MPa, whereas β-lg was denatured at pressures >100 MPa. Denaturation of α-la and β-lg increased with increasing pressure, treatment time and temperature and milk pH. The majority of denatured β-lg was apparently associated with casein micelles. These effects of HP on casein micelles and whey proteins in milk may have significant implications for properties of products made from HP-treated milk.

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Monte Carlo analysis of the product handling and high-pressure treatment effects on the Vibrio vulnificus risk to raw oysters consumers

Journal of Food Engineering ◽

10.1016/j.jfoodeng.2014.07.014 ◽

2015 ◽

Vol 144 ◽

pp. 86-92 ◽

Cited By ~ 6

Author(s):

Vinicio Serment-Moreno ◽

Kai Deng ◽

Xulei Wu ◽

Yi-Cheng Su ◽

Claudio Fuentes ◽

...

Keyword(s):

High Pressure ◽

Monte Carlo ◽

Treatment Effects ◽

Vibrio Vulnificus ◽

Monte Carlo Analysis ◽

Pressure Treatment ◽

High Pressure Treatment

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Ultra-high pressure treatment effects on polysaccharides and lignins of longan fruit pericarp

Food Chemistry ◽

10.1016/j.foodchem.2008.05.097 ◽

2009 ◽

Vol 112 (2) ◽

pp. 428-431 ◽

Cited By ~ 58

Author(s):

Bao Yang ◽

Yueming Jiang ◽

Rui Wang ◽

Mouming Zhao ◽

Jian Sun

Keyword(s):

High Pressure ◽

Treatment Effects ◽

Pressure Treatment ◽

High Pressure Treatment ◽

Ultra High Pressure ◽

Fruit Pericarp

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Thermal processing, salt and high pressure treatment effects on molecular structure and antigenicity of sesame protein isolate

Food Research International ◽

10.1016/j.foodres.2013.04.016 ◽

2013 ◽

Vol 53 (1) ◽

pp. 240-251 ◽

Cited By ~ 30

Author(s):

Allaoua Achouri ◽

Joyce Irene Boye

Keyword(s):

Molecular Structure ◽

High Pressure ◽

Thermal Processing ◽

Treatment Effects ◽

Protein Isolate ◽

Pressure Treatment ◽

High Pressure Treatment

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High-Pressure Treatment Effects on Food Proteins of Animal Origin

Novel Food Processing ◽

10.1201/9781420071221-19 ◽

2016 ◽

pp. 275-298

Keyword(s):

High Pressure ◽

Treatment Effects ◽

Animal Origin ◽

Pressure Treatment ◽

Food Proteins ◽

High Pressure Treatment

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Binding of curcumin to milk proteins increases after static high pressure treatment of skim milk

Journal of Dairy Research ◽

10.1017/s0022029913000125 ◽

2013 ◽

Vol 80 (2) ◽

pp. 152-158 ◽

Cited By ~ 16

Author(s):

Saeed Rahimi Yazdi ◽

Francesco Bonomi ◽

Stefania Iametti ◽

Matteo Miriani ◽

Andrea Brutti ◽

...

Keyword(s):

High Pressure ◽

Skim Milk ◽

Milk Proteins ◽

Pressure Treatment ◽

Amino Acid Residues ◽

Casein Micelles ◽

High Pressure Treatment ◽

Structural Modifications ◽

Close Proximity ◽

Hydrophobic Nature

Curcumin is a bioactive polyphenolic compound extracted from turmeric with known anti-inflammatory properties, and its hydrophobic nature restricts its solubility and its bioaccessibility. Solubility may be improved upon binding of curcumin to native or treatment-modified casein micelles. The present work demonstrated that high hydrostatic pressure treatment of skim milk increases the binding of curcumin to caseins. The association of curcumin to casein micelles was assessed using fluorescence spectroscopy, either directly or by tryptophan quenching. The amount of curcumin associated with the milk proteins increased in pressure-treated milk, and a further improvement in the amount of bound curcumin was observed upon pressure treatment of a milk/curcumin mixture. However, in this case, some of the curcumin dissociated during storage, contrarily to what was observed for untreated milk. From a molecular standpoint, the data presented here indicate that structural modifications induced by high-pressure treatment and known to affect the structure of milk proteins result in a rearrangement of the amino acid residues in close proximity to the protein-associated curcumin.

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