Structural effects on the permeability of whey protein films in an aqueous environment

Bodnár, Igor; Alting, Arno C.; Verschueren, M.

doi:10.1016/j.foodhyd.2006.11.017

Cited by 21 publications

(17 citation statements)

References 19 publications

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“…Under almost neutral conditions, aggregation is irreversibly induced by heat through a three-step process (Bodnár et al, 2007): (1) initiation, (2) propagation, and (3) termination. During initiation, the free SH groups that are normally buried at the interface between native monomers, become exposed to further re-action (Zuniga et al, 2010).…”

Section: Effect Of Environmental Factors On Protein Aggregationmentioning

confidence: 99%

“…Each of these processes induces partial (or total) unfolding of the native structure of proteins, thus resulting in protein aggregation and eventual gel formation. Without a heating step, protein networks will hardly form while remaining stable in water (Bodnár, Alting, & Verschueren, 2007;Pérez-Gago, Nadaud, & Krochta, 1999;Ramos et al, 2012). Once whey proteins have been heated to a temperature leading to the onset of denaturation, they start to unfold (see Table 1) -and may form different types of aggregates (e.g.…”

mentioning

confidence: 99%

“…In turn, the reactive dimer can react similarly with a non-denatured monomer, and this propagation step can be repeated several times, thus increasing the size of the polymer chain. These aggregates apparently assume a linear organization due conformation of β-Lg and conformational changes occurring during propagationonly one of the two intra-molecular disulfide bonds and only one SH group/monomer are supposed to be reactive (Bodnár et al, 2007). Finally, aggregation stops (termination step) when two active intermediates (i.e.…”

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confidence: 99%

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Physical effects upon whey protein aggregation for nano-coating production

Ramos

Pereira

Rodrigues

et al. 2014

Food Research International

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Section: Effect Of Environmental Factors On Protein Aggregationmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Physical effects upon whey protein aggregation for nano-coating production

Ramos

Pereira

Rodrigues

et al. 2014

Food Research International

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“…There is large information available on the barrier and mechanical properties of whey protein-based films (Bodnár, Alting, & Verschueren, 2007;Fairley et al, 1996a,b;Krochta & de MulderJohnston, 1997;McHugh & Krochta, 1994a), but little information exists on the molecular structure of those films; hence, this work contributed to elucidate the relationships between barrier, tensile, surface and thermal features by providing data on said molecular structure, especially within wide ranges of Gly content. The aforementioned fundamental relationships are crucial to optimize film composition in a rational manner (in terms of protein feedstock and Gly level) toward pre-specified physical properties.…”

Section: Introductionmentioning

confidence: 99%

Effect of whey protein purity and glycerol content upon physical properties of edible films manufactured therefrom

Ramos

Reinas²,

Silva³

et al. 2013

Food Hydrocolloids

397

216

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a b s t r a c tThis manuscript describes the detailed characterization of edible films made from two different protein products e whey protein isolate (WPI) and whey protein concentrate (WPC), added with three levels of glycerol (Gly) e i.e. 40, 50 and 60%(w/w). The molecular structure, as well as barrier, tensile, thermal, surface and optical properties of said films were determined, in attempts to provide a better understanding of the effects of proteinaceous purity and Gly content of the feedstock. WPI films exhibited statistically lower (p < 0.05) moisture content (MC), film solubility (S), water activity, water vapor permeability (WVP), oxygen and carbon dioxide permeabilities (O 2 P and CO 2 P, respectively) and color change values, as well as statistically higher (p < 0.05) density, surface hydrophobicity, mechanical resistance, elasticity, extensibility and transparency values than their WPC counterparts, for the same content of Gly. These results are consistent with data from thermal and FTIR analyses. Furthermore, a significant increase (p < 0.05) was observed in MC, S, WVP, O 2 P, CO 2 P, weight loss and extensibility of both protein films when the Gly content increased; whereas a significant decrease (p < 0.05) was observed in thermal features, as well as in mechanical resistance and elasticity e thus leading to weaker films. Therefore, fundamental elucidation was provided on the features of WPI and WPC germane to food packaging e along with suggestions to improve the most critical ones, i.e. extensibility and WVP.

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“…Therefore, the aggregation process in whey proteins is usually preceded by a step to favor the denatured state; without this step, protein network structures would be harder to achieve and once formed remain hardly stable in water (Perez-Gago et al, 1999;Bodn ar et al, 2007;Ramos et al, 2012a). A quantitatively kinetic model for the temperature-induced denaturation and aggregation of -Lg, in almost neutral conditions, has been previously presented (Roefs and De Kruif, 1994).…”

Section: Aggregationmentioning

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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Structural effects on the permeability of whey protein films in an aqueous environment

Cited by 21 publications

References 19 publications

Physical effects upon whey protein aggregation for nano-coating production

Physical effects upon whey protein aggregation for nano-coating production

Effect of whey protein purity and glycerol content upon physical properties of edible films manufactured therefrom

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

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