The Adsorption of Whey Proteins on the Surface of Emulsified Fat

Shimizu, Makoto; Kamiya, T.; Yamauchi, Kunio

doi:10.1080/00021369.1981.10864922

Cited by 33 publications

(43 citation statements)

References 5 publications

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“…First, it has been reported that α s1 -casein, one of the major proteins in caseinate, does not form intermolecular calcium cross-links in solution (17), whereas -Lg does (27,28). Also, exposure of hitherto buried hydrophobic regions as -Lg binds and unfolds at the interface (29) would enhance aggregation as soon as electrostatic repulsions between the particles were reduced by calcium binding. This relative sensitivity could also depend on the distribution of the major binding sites for Ca 2 + in the different proteins.…”

Section: Discussionmentioning

confidence: 98%

Kinetics of the Calcium-Induced Instability of Oil-in-Water Emulsions: Studies Under Quiescent and Shearing Conditions

Agboola

Dalgleish

1996

LWT - Food Science and Technology

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Section: Discussionmentioning

confidence: 98%

Kinetics of the Calcium-Induced Instability of Oil-in-Water Emulsions: Studies Under Quiescent and Shearing Conditions

Agboola

Dalgleish

1996

LWT - Food Science and Technology

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“…On the other hand, the higher value of P ads L than P ads SDS could be explained by the fact that P ads L takes into account both tightly and loosely adsorbed proteins (i.e. all the layers of adsorbed proteins on the fat globules' surface), as reported by Shimizu et al [46] from simple milk protein-based emulsions. However, evaluation of the percentage of adsorbed proteins using P ads SDS values considers only tightly adsorbed proteins which are desorbed by SDS molecules, from extensively washed creams.…”

Section: Amount Of Adsorbed Protein and Fat Protein Loadmentioning

confidence: 91%

“…In the present study, we also considered the proteins which were desorbed from the washed cream by SDS molecules (P ads SDS ). The last method has been previously applied to simple emulsions stabilized by caseinate or whey proteins [9,28,45,46] and to ice cream model mixes [3]. In the present study, the final washed cream layer was dispersed in 5% w/w SDS with (reducing conditions) or without (non-reducing conditions) 2-mercaptoethanol (2.5% w/w), stirred at room temperature to desorb proteins [13,28], and then centrifuged in the conditions described above.…”

Section: Analysis Of Adsorbed Proteinmentioning

confidence: 99%

“…The molecular mechanisms responsible for storage stability in model emulsions have already been studied through analysis of the droplet size distribution and protein composition of either the aqueous phase or the fat surface layer [5,6,17,19,21,28,46,47,49]. In complex emulsions [2,3,[22][23][24][25] as well as in model emulsions [13,17,21,47], competitive adsorption of proteins and emulsifiers for the oil-water interface was also reported.…”

Section: Introductionmentioning

confidence: 99%

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Composition of fat protein layer in complex food emulsions at various weight ratios of casein-to-whey proteins

Sourdet¹,

Relkin²,

Fosseux

et al. 2002

Lait

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-We studied three complex food emulsions which differed only by the weight ratio of casein-to-whey proteins (80:20, 60:40, 0:100). We considered the stability of the fat droplets against aggregation/coalescence, the amount of adsorbed proteins, and the protein composition of the interface. Our results indicated that coalescence was inhibited whatever the protein composition. However, aggregation between fat droplets was observed in the casein-free emulsion (0:100), where the amount of adsorbed proteins at the fat globule surface was the lowest. Quantitative SDS-PAGE experiments showed that preferential adsorption of caseins over globular proteins occurs only in the emulsion based on the intermediate (60:40) casein-to-whey protein ratio. Furthermore, the proportion of adsorbed proteins which were found in polymeric forms seemed to increase with decreasing casein-to-whey protein ratio. The fat globule stability, total fat protein load and proportion of adsorbed protein in the polymeric forms were discussed in terms of adsorption properties of milk proteins at the oil-water interface, in relation to the casein-to-whey protein ratio.Milk protein / emulsion / stability / protein adsorption / disulfide bond Résumé -Composition de la couche protéique adsorbée à la surface des globules gras dans des émulsions alimentaires complexes contenant différents rapports caséine/protéines sériques. Nous avons étudié trois émulsions alimentaires complexes qui ne diffèrent entre elles que par le rapport massique caséine/protéines sériques (80:20 ; 60:40 et 0:100). Cette étude a été réalisée en considérant la stabilité des gouttelettes lipidiques vis-à-vis de l'agrégation/coalescence, la quantité de protéines adsorbées par unité de surface de globule gras et la composition de l'interface. Nos résultats ont montré l'absence de coalescence dans les trois émulsions, et la présence d'agrégats n'a été observée que dans l'émulsion (0:100) ne contenant pas de caséine. Dans ce dernier cas, la quantité de protéines adsorbées à la surface des globules gras est la plus faible. Une étude quantitative par électro-phorèse sur gel de polyacrylamide a indiqué une adsorption préférentielle des caséines par rapport aux protéines sériques dans le cas de l'émulsion préparée à base du ratio intermédiaire (60:40) de caséine/protéines sériques. De plus, la proportion de polymères adsorbés à la surface de globules gras semble augmenter lorsque le rapport massique caséine/protéiques sériques diminue. La stabilité des émulsions, la charge protéique des globules gras et la proportion de polymères adsorbés sont discutées en fonction du rapport caséine/protéines sériques.Protéine laitière / émulsion / stabilité / adsorption des protéines / pont disulfure

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“…20 ) We have found that adsorbed whey proteins including [3-Lg on emulsified oil surfaces were more easily digested with proteases than the native whey proteins. 6 ) This suggests that whey proteins are denatured on the oil surface. Denaturability of proteins might, therefore, be an important factor affecting their emulsifying properties.…”

Section: Denaturability Of [3-lg At Different Phsmentioning

confidence: 99%