Hydrophilic lecithins protect milk proteins against heat-induced aggregation

Le, T. Tran; El-Bakry, M.; Neirynck, Nico; Boguś, Mieczysława I.; Hoa, H. Dinh; Meeren, Paul Van der

doi:10.1016/j.colsurfb.2007.06.007

Cited by 29 publications

(9 citation statements)

References 29 publications

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“…From Table 2, DLS clearly indicates that the average hydrodynamic diameter is largely increased upon heating a concentrated casein micellar dispersion in the presence of whey proteins. In fact, the increase in diameter was much higher as compared with the results found by Anema and Li (2003b), which is a logical consequence of the higher overall protein concentration as well as the higher whey protein to casein ratio in our model system (Tran Le et al, 2007): these authors observed an increase by up to 30 nm at pH 6.55, whereas only a 10 nm increase was reported at pH 6.7 in heated reconstituted skim milk.…”

Section: Particle Size Distribution Of Casein Micellar Dispersionscontrasting

confidence: 78%

“…In addition, we wanted to find an answer to the question of whether the increase in average particle size was due either to whey protein deposition itself, or to the concomitant casein micellar aggregation. Hereby, the composition of the model system was optimized to promote heat-induced dairy protein interactions by combining a higher overall protein content with a higher whey protein to casein ratio than normally encountered in milk (Tran Le et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Determination of heat-induced effects on the particle size distribution of casein micelles by dynamic light scattering and nanoparticle tracking analysis

Saveyn

Hoa

et al. 2008

International Dairy Journal

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Section: Particle Size Distribution Of Casein Micellar Dispersionscontrasting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Determination of heat-induced effects on the particle size distribution of casein micelles by dynamic light scattering and nanoparticle tracking analysis

Saveyn

Hoa

et al. 2008

International Dairy Journal

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“…Other studies also indicated that ligands or surfactants like arginine, guanidium, lecithins, SDS or sodium laurate could control over-aggregation of heat-induced complexes of milk proteins (Tran Le et al 2007;Unterhaslberger et al 2006). Kerstens et al (2005) reported a peculiar effect of the non-ionic surfactant Tween 20, which promotes formation of μm-large, spherical, sizedesigned, reversible heat-induced aggregates in concentrated β-LG solutions.…”

Section: Possible Methods To Modify the Size Of The Heat-induced Wheymentioning

confidence: 96%

How to tailor heat-induced whey protein/κ-casein complexes as a means to investigate the acid gelation of milk—a review

Morand

Guyomarc’H

Famelart

2011

Dairy Science & Technol.

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The heat treatment of milk greatly improves the acid gelation of milk and is therefore largely applied in yoghurt manufacture. During the heat treatment, soluble and micelle-bound whey protein/κ-casein complexes are produced in milk. The complexes and their physico-chemical properties have been held responsible for the early gelation point, the increased final firmness and for the serum retention capacity of the acid gels made of heated milk. They are suspected to bring new functionalities to the casein micelles and to help the formation of interactions when building the gel network. In order to investigate the type of interactions that the complexes can affect throughout the acid gelation of milk, an original strategy would be to control the physico-chemical properties of the whey protein/κ-casein soluble complexes and to use them as vectors to modify the possible interactions in the milk. In that perspective, the different physico-chemical properties of the whey protein/κ-casein soluble complexes that are thought to significantly affect the acid gelation behaviour of the casein micelles are listed. Then, the physical, chemical and biological means that could possibly be applied to the formation of complexes in order to modulate each of the targeted property are reviewed and evaluated. In order to open a large choice for future investigation, these methods were found in a larger literature resource than milk, including other protein systems like model whey protein solutions or non-dairy globular protein systems. The food-compatible

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“…This gives suprastructures that differ significantly, at least by the type of interactions maintaining proteins together in the aggregates, from the ones obtained in the absence of copper (Gulzar et al 2009). In the presence of molecules often recovered in milk protein ingredients such as fatty acids (Le Maux et al 2012), or phospholipids (Le et al 2007), the aggregation behavior of the proteins is changed on heating. These examples indicate that controlling the structure of whey protein aggregates is difficult in complex systems even though the structure of the building blocks (native whey proteins) is well known.…”

Section: Conclusion: Perspectivesmentioning

confidence: 99%

Current ways to modify the structure of whey proteins for specific functionalities—a review

Guyomarc’H

Famelart

Henry

et al. 2014

Dairy Sci. & Technol.

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The native whey proteins have been intensively used in a multitude of food applications due to their high nutritional, biological, and versatile technofunctional properties. The range of applications of whey proteins has further been extended in the last decades by the use of whey protein aggregates offering new technofunctional properties. These properties are directly dependent on the structure of whey protein aggregates, i.e., their size, shape, density, surface properties, and the type of bonds maintaining proteins together in the aggregates. In this review, after a brief description of the major whey proteins, we examine the most important advances reported to date pertaining to the available approaches to modify the structure of whey proteins for specific functionalities. Our laboratory, Science and Technology of Milk and Eggs, has contributed significantly to the advancement of knowledge on the structure-function relationships of whey proteins either in the native or denatured/aggregated forms. Our expertise and research approaches are highlighted throughout some selected results accumulated during the last decade in comparison with results from the literature.

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Hydrophilic lecithins protect milk proteins against heat-induced aggregation

Cited by 29 publications

References 29 publications

Determination of heat-induced effects on the particle size distribution of casein micelles by dynamic light scattering and nanoparticle tracking analysis

Determination of heat-induced effects on the particle size distribution of casein micelles by dynamic light scattering and nanoparticle tracking analysis

How to tailor heat-induced whey protein/κ-casein complexes as a means to investigate the acid gelation of milk—a review

Current ways to modify the structure of whey proteins for specific functionalities—a review

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