Changing the isoelectric point of the heat-induced whey protein complexes affects the acid gelation of skim milk

Morand, Marion; Guyomarc’H, Fanny; Legland, David; Famelart, Marie-Hélène

doi:10.1016/j.idairyj.2011.10.006

Cited by 39 publications

(31 citation statements)

References 30 publications

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“…The degree of acylation of the samples was assayed using orthophthaldialdehyde (OPA) as described previously by Morand et al (2012). In presence of 2-dimethylaminoethanothiol hydrochloride (DMA), OPA reacts with the free primary amino groups of proteins and yields alkyl-iso-indole derivates that absorb light at 340 nm.…”

Section: Evaluation Of the Degree Of Modificationmentioning

confidence: 99%

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

Morand

Dekkari

Guyomarc’H

et al. 2012

International Dairy Journal

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Section: Evaluation Of the Degree Of Modificationmentioning

confidence: 99%

“…In line with this hypothesis, Morand, Guyomarc'h, Legland, and Famelart (2012) chemically modified the apparent isoelectric point (pI) of heat-induced whey protein complexes to assess the role of electrostatic repulsion on the acid gelation of skim milk. The results…”

Section: Introductionmentioning

confidence: 99%

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

Morand

Dekkari

Guyomarc’H

et al. 2012

International Dairy Journal

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“…Light microscopy, such as Confocal Laser Scanning Microscopy (CLSM), allows the observation of dairy products with a minimum of sample preparation and with a resolution up to 0.25 microns (Ercili-Cura et al, 2013;Fenoul, Le Denmat, Hamdi, Cuvelier, & Michon, 2008;Morand, Guyomarc'h, Legland, & Famelart, 2012). By using this technique, it may be possible to distinguish the structure of the milk gel, but not the fine organisation of casein micelles that form its microstructure.…”

Section: Introductionmentioning

confidence: 99%

“…When a protein network cannot be easily segmented, gray level texture analysis can be used to discern the variations of gray levels from confocal images (Ercili-Cura et al, 2013;Fenoul et al, 2008;Morand et al, 2012). An alternative to particle-based image analysis and image texture analysis is the characterization of protein network as a binary microstructure.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the microstructure of dairy systems using automated image analysis

et al. 2015

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International audienceA sound understanding of the microstructure of dairy products is of great importance in order to predict and control their properties and final quality. The aim of this study was to develop an automated image analysis procedure to characterize the microstructure of different dairy systems. A high pressure freezing coupled with freeze-substitution (HPF-FS) protocol was applied prior to transmission electron microscopy(TEM) in order to minimize any modification of the microstructure of the dairy systems investigated. The developed image analysis procedure was first validated on synthetic images of suspensions, and then on two types of concentrated milk suspensions. Microstructural data relating to casein micelles in milk suspensions were taken from the literature. The established procedure was then applied to the two corresponding rennet-induced milk gels, prepared from the same milk concentrates used for suspensions preparation. The automated image analysis procedure allowed the reliable estimation of several characteristic microstructural parameters including area fraction, porosity, boundary length per unit area, particle aggregate size, inter-particle aggregate distance and tortuosity. The relative ease of estimating these microstructural parameters from the automated image analysis method could make it useful for routine measurements of milk gels. Moreover, the method enabled a useful discrimination between two different types of milk gels. This novel approach can contribute to a better understanding of the effects of processing on the structure-property relationships in dairy products, and may be applied to other food systems

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“…In another paper, Morand et al (2012b) produced whey protein aggregates by heating whey protein solutions in the same conditions as used by Vasbinder et al (2004), i.e., 68.5°C for 2 h. Then the surface charge of the aggregates was modified by succinylation or methylation. The grafting of a succinyl group on the lysine residues or of a methyl group on carboxyl groups of proteins, respectively, reduced or increased the pI of the aggregates due to the substitution of a positive group by a negative one, or to the neutralization of a negative group, respectively.…”

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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Changing the isoelectric point of the heat-induced whey protein complexes affects the acid gelation of skim milk

Cited by 39 publications

References 30 publications

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

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

Characterization of the microstructure of dairy systems using automated image analysis

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

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