Spontaneous Assembly and Induced Aggregation of Food Proteins

Bouhallab, Saı̈d; Croguennec, Thomas

doi:10.1007/12_2012_201

Cited by 23 publications

(34 citation statements)

References 139 publications

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“…In particular, fibrillary like aggregates (d f → 1) significantly increase the viscosity of the suspension even at low protein volume fractions, while dense spherical aggregates (d f → 3) have a smaller impact on viscosity even at higher volume fractions [95]. Moreover, the same protein can lead to different structures (i.e., rods, spheres or branched, flexible strands) according to the environmental conditions employed (pH, ionic strength, protein concentration), as in the case of the whey protein isolate or beta-lactoglobulin [96].…”

Section: Food Productsmentioning

confidence: 99%

“…Moreover, the same protein can lead to different structures (i.e., rods, spheres or branched, flexible strands) according to the environmental conditions employed (pH, ionic strength, protein concentration), as in the case of the whey protein isolate or beta-lactoglobulin [96]. Controlling size and shape of protein aggregates is of key importance as for instance the presence of micron-sized globular aggregates results in a coarse mouth feeling texture [95].…”

Section: Food Productsmentioning

confidence: 99%

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Fractal-like structures in colloid science

Lazzari

Nicoud

Jaquet

et al. 2016

Advances in Colloid and Interface Science

175

126

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a b s t r a c tThe present work aims at reviewing our current understanding of fractal structures in the frame of colloid aggregation as well as the possibility they offer to produce novel structured materials. In particular, the existing techniques to measure and compute the fractal dimension d f are critically discussed based on the cases of organic/inorganic particles and proteins. Then the aggregation conditions affecting d f are thoroughly analyzed, pointing out the most recent literature findings and the limitations of our current understanding. Finally, the importance of the fractal dimension in applications is discussed along with possible directions for the production of new structured materials.

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Section: Food Productsmentioning

confidence: 99%

Section: Food Productsmentioning

confidence: 99%

Fractal-like structures in colloid science

Lazzari

Nicoud

Jaquet

et al. 2016

Advances in Colloid and Interface Science

175

126

View full text Add to dashboard Cite

show abstract

“…Protein concentration, time and temperature of heating, pH, and the presence of specific ions are the main factors affecting the dimensions of the assemblies. Some results briefly presented below on the dimensions of heat-induced assemblies of whey proteins were mainly obtained on studies conducted on β-LG and are extensively detailed in recent reviews (Nicolai et al 2011;Nicolai and Durand 2013;Bouhallab and Croguennec 2014).…”

Section: Form Factor Size and Densitymentioning

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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“…Whey nanofibrils can entangle to form physical nanohydrogels at relatively low protein concentrations. Fibril formation may involve several steps, including exposition of hydrophobic regions and preservation of some native surface charges besides reversible formation of linear aggregates, followed by a slow process of "consolidation", after which fibrils no longer disintegrate upon subsequent slow cooling (Arnaudov et al, 2003;Bouhallab and Croguennec, 2014). The fibrillation process can be favored by cleavage of some peptide bonds, and give rise to other supra-molecular structures such as ribbons, spherulites, and nanotubes (Akkermans et al, 2008;Tavares et al, 2014).…”

Section: Nanofibrilsmentioning

confidence: 99%

Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food

Ramos

Pereira

Martins

et al. 2017

Critical Reviews in Food Science and Nutrition

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Whey proteins are widely used as nutritional and functional ingredients in formulated foods because they are relatively inexpensive, generally recognized as safe (GRAS) ingredient, and possess important biological, physical, and chemical functionalities. Denaturation and aggregation behavior of these proteins is of particular relevance toward manufacture of novel nanostructures with a number of potential uses. When these processes are properly engineered and controlled, whey proteins may be formed into nanohydrogels, nanofibrils, or nanotubes and be used as carrier of bioactive compounds. This review intends to discuss the latest understandings of nanoscale phenomena of whey protein denaturation and aggregation that may contribute for the design of protein nanostructures. Whey protein aggregation and gelation pathways under different processing and environmental conditions such as microwave heating, high voltage, and moderate electrical fields, high pressure, temperature, pH, and ionic strength were critically assessed. Moreover, several potential applications of nanohydrogels, nanofibrils, and nanotubes for controlled release of nutraceutical compounds (e.g. probiotics, vitamins, antioxidants, and peptides) were also included. Controlling the size of protein networks at nanoscale through application of different processing and environmental conditions can open perspectives for development of nanostructures with new or improved functionalities for incorporation and release of nutraceuticals in food matrices.

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Spontaneous Assembly and Induced Aggregation of Food Proteins

Cited by 23 publications

References 139 publications

Fractal-like structures in colloid science

Fractal-like structures in colloid science

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

Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food

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