Increasing the hydrophobicity of the heat-induced whey protein complexes improves the acid gelation of skim milk

Morand, Marion; Dekkari, Assiba; Guyomarc’H, Fanny; Famelart, Marie-Hélène

doi:10.1016/j.idairyj.2012.03.002

Cited by 37 publications

(7 citation statements)

References 38 publications

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“…Furthermore, hydrophobic interactions of neutral protein molecules can become more preponderant to encourage the aggregation and lead to formation of more compact aggregates (Kohyama et al, 1995). Morand et al (2012) founded that the high surface hydrophobicity of the whey protein complexes, or model milk influenced the microstructure of the acid gels which gave earlier and firmer.…”

Section: Change In Secondary Tertiary Structures and Sds-page Of Processed Milk Samples 1fluorescence Spectroscopymentioning

confidence: 99%

“…While the hydrophobic regions of protein molecules are in the original state inside and exposed to the outside by heat denaturation ( Kohyama et al, 1995). (Kohyama et al, 1995;Morand et al, 2012) suggested that, the hydrophobic interaction fundamentally plays a role in the acid gel structure formation. However, heat treatment is the most common methods for preserving food products, thermosonication could be applied as a substitutional process to heat treatment.…”

Section: Introductionmentioning

confidence: 99%

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Textural and Microstructural Properties of Set Yoghurt Produced from Goat Milk Treated by Homogenization and Thermosonication

Ragab

Yacoub

Nassar

et al. 2021

Alexandria Science Exchange Journal

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Thermosonication (TS) prior to conventionally heated (95 o C for 10 min) goat milk (GM) (at an ultrasound frequency of 20 kHz and output power 4000 W, from 5 to 15 min) effected the preparation of yoghurts with microstructure and texture properties superior to those of control yoghurt samples produced from homogenization milk (HM) before heated at the same temperature. Thermosonication altered the secondary structure of the protein which decreased β-sheet content and increased the amount of α-helix structure leading to increase the hydrophobicity. As well as in thermosonication milk (TSM) samples, the percentage of β-sheet structures inversely correlated with the exposure of hydrophobic regions of the protein (r = 0.79; r = 0.84), while the percentage of α-helix structure positively correlated to the increase in the surface hydrophobicity (r = 0.61; r = 0.92) for GM and cow milk (CM) samples, respectively. Moreover, there were no significant aggregates observed in TS samples compared to the homogenized, before heating. Texture profile and microstructure analysis showed that the yoghurt produced from the thermosonication milk samples had higher firmness, adhesiveness, and deluxe network structure than those induced from the homogenized milk samples.

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Section: Change In Secondary Tertiary Structures and Sds-page Of Processed Milk Samples 1fluorescence Spectroscopymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Textural and Microstructural Properties of Set Yoghurt Produced from Goat Milk Treated by Homogenization and Thermosonication

Ragab

Yacoub

Nassar

et al. 2021

Alexandria Science Exchange Journal

View full text Add to dashboard Cite

show abstract

“…In addition, a higher concentration of κ-CN, particularly G-κ-CN (both highest in the late season), might reduce the hydrophobicity of the protein matrix, weakening the hydrophobic interactions in the acid gel network. The importance of hydrophobic interactions in the development of acid milk gel structure has been well established (Jean et al, 2006;Donato and Guyomarc'h, 2009;Morand et al, 2012).…”

Section: Correlation and Interpretationmentioning

confidence: 99%

Effect of seasonal variations on the acid gelation of milk

Singh

2020

Journal of Dairy Science

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We investigated the effect of seasonal variations on the acid gelation properties of bovine milk in a seasonal-calving New Zealand herd for 2 full milking seasons. We tested the formation of acid gels in 2 milk systems: unstandardized skim milk and standardized whole milk (4.6% protein, 4.0% fat). For unstandardized skim milk, late-season milk acid gels had a longer gelation time and a lower gelation pH than early-and mid-season milk acid gels, but we found no consistent seasonal variation in the final storage modulus. For standardized milk, late-season milk had the most inferior acid gelation properties during the year, including the lowest final storage modulus, the lowest gelation pH, and the longest gelation time. Standardization alleviated but did not eliminate the prolonged gelation time of late-season milk. These results indicated that the physicochemical properties of seasonal milk contributed greatly to its acid gelation, independent of differences in protein content. Standardization was not adequate to stabilize the acid gelation properties of late-season milk. Desirable acid gelation properties correlated with lower glycosylated κ-casein content, lower β-lactoglobulin:α-lactalbumin ratio, lower extent of whey protein-casein micelle association, and lower total calcium and ionic calcium content. We discuss the possible effects of the correlating variables on the acid gelation properties of seasonal milk. Natural variations in the glycosylation degree of κ-casein might play an important role in acid gel structural development by altering the electrostatic and hydrophobic interactions among the milk proteins.

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“…To evaluate the contribution of the aggregate's surface hydrophobicity on acid gelation of dairy mixtures, Morand et al (2012a) produced heat-induced whey protein aggregates that were modified by grafting with chemical groups of ranged hydrophobicity. Whey protein aggregates were either succinylated using succinic anhydride or acylated using acetic, butanoic, or hexanoic anhydrides in order to obtain aggregates of increasing order of hydrophobicity.…”

Section: Surface Propertiesmentioning

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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Increasing the hydrophobicity of the heat-induced whey protein complexes improves the acid gelation of skim milk

Cited by 37 publications

References 38 publications

Textural and Microstructural Properties of Set Yoghurt Produced from Goat Milk Treated by Homogenization and Thermosonication

Textural and Microstructural Properties of Set Yoghurt Produced from Goat Milk Treated by Homogenization and Thermosonication

Effect of seasonal variations on the acid gelation of milk

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

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