Emulsification properties of whey proteins in their natural environment: effect of whey protein concentration at 4 and 18% milk fat

McCrae, Catharina H.; Law, Andrew J. R.; Leaver, J. D.

doi:10.1016/s0268-005x(99)00024-7

Cited by 14 publications

(12 citation statements)

References 24 publications

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“…Such a result is in accordance with previous studies describing that a-lactalbumin was absorbed better on the oil droplets than b-lactoglobulin in acid pH [11,13]. The similarity between emulsifying activities of these two native proteins at neutral pH agrees well with the results of McCrae et al [2]. The stability of emulsion made from native a-lactalbumin at pH 5 is bigger than that obtained with b-lactoglobulin.…”

Section: Emulsifying Propertiessupporting

confidence: 92%

“…Since protein concentration play an important role in emulsifying activity [2,26], preliminary experiment was carried out in order to compare emulsions obtained using 2 and 4 mg/ml of native and methylated b-lactoglobulin (data not shown). There was no effect of protein concentration when using native Table 1.…”

Section: Emulsifying Propertiesmentioning

confidence: 99%

“…Hence, they are used as ingredients in a wide range of food products [1,2]. Due to its amphiphilic properties, b-casein is one of the most tension active milk proteins [3,4].…”

Section: Introductionmentioning

confidence: 99%

“…Adsorption of b-lactoglobulin on the oil/water interfacial layer is strongly reduced with decreasing pH reaching 61.6 and 12.9% at pH 9 and 3, respectively. This can be attributed to pH-dependent structural changes since b-lactoglobulin molecules are more rigid at acid pH [2,8,9]. Recently, it was confirmed that pH influences the interfacial composition and stability of emulsions prepared from egg yolk proteins [10].…”

Section: Introductionmentioning

confidence: 99%

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Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification

Sitohy

Chobert²,

Haertlé³

2001

Nahrung

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Three milk proteins (beta-lactoglobulin, alpha-lactalbumin and beta-casein) were esterified to different extents with methanol, ethanol and propanol, then their solubility was studied in the pH-range of 3-10. Their emulsifying properties were also checked in the pH-range of 3-7 by measuring the oil-droplet size using laser light scattering. Solubility of all esterified proteins was improved in the acidic pH range (3-6). The magnitude of improvement was depending on the extent of esterification, the nature of the grafted ester group and the nature of the modified protein. Emulsifying activity and stability of esterified milk proteins in the acidic pH range of 3-5 were generally higher compared to the corresponding native proteins. This improvement was associated with the degree of solubility, the degree of esterification, the type of ester group grafted and the nature of the used protein. The highest emulsifying activity improvement was observed for methyl ester derivatives at pH 5 where the native proteins have poor emulsifying properties.

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Section: Emulsifying Propertiessupporting

confidence: 92%

Section: Emulsifying Propertiesmentioning

confidence: 99%

“…Hence, they are used as ingredients in a wide range of food products [1,2]. Due to its amphiphilic properties, b-casein is one of the most tension active milk proteins [3,4].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification

Sitohy

Chobert²,

Haertlé³

2001

Nahrung

View full text Add to dashboard Cite

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“…Skim milk powder, sweet buttermilk (BM) powder, butter-derived serum phase, whey proteins, casein dispersions, phospholipids, and purified milk fat globule membrane (MFGM) suspensions have been successfully used to make emulsions (Tomas and Paquet, 1994;Elling et al, 1996;McCrae et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Comparison of emulsifying properties of milk fat globule membrane materials isolated from different dairy by-products

Phan

Meeren

et al. 2014

Journal of Dairy Science

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Emulsifying properties of milk fat globule membrane (MFGM) materials isolated from reconstituted buttermilk (BM; i.e., BM-MFGM) and BM whey (i.e., whey-MFGM), individually or in mixtures with BM powder (BMP) were compared with those of a commercial dairy ingredient (Lacprodan PL-20; Arla Foods Ingredients Group P/S, Viby, Denmark), a material rich in milk polar lipids and proteins. The particle size distribution, viscosity, interfacial protein, and polar lipids load of oil-in-water emulsions prepared using soybean oil were examined. Pronounced droplet aggregation was observed with emulsions stabilized with whey-MFGM or with a mixture of whey-MFGM and BMP. No aggregation was observed for emulsions stabilized with BM-MFGM, Lacprodan PL-20, or a mixture of BM-MFGM and BMP. The surface protein load and polar lipids load were lowest in emulsions with BM-MFGM. The highest protein load and polar lipids load were observed for emulsions made with a mixture of whey-MFGM and BMP. The differences in composition of MFGM materials, such as in whey proteins, caseins, MFGM-specific proteins, polar lipids, minerals, and especially their possible interactions determine their emulsifying properties.

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Whey Protein-Based Functional Energy Drinks Formulation and Characterization

Mehmood

Iyer

Arif

et al. 2019

Sports and Energy Drinks

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Emulsification properties of whey proteins in their natural environment: effect of whey protein concentration at 4 and 18% milk fat

Cited by 14 publications

References 24 publications

Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification

Improvement of solubility and of emulsifying properties of milk proteins at acid pHs by esterification

Comparison of emulsifying properties of milk fat globule membrane materials isolated from different dairy by-products

Whey Protein-Based Functional Energy Drinks Formulation and Characterization

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