Changes in structure and functional properties of whey proteins induced by high hydrostatic pressure: A review

Liu, Xiaoming; Jia, Ning; Clark, Stephanie

doi:10.1007/s11705-009-0251-0

Cited by 7 publications

(4 citation statements)

References 60 publications

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“…Whey protein is a general term for various protein components from whey. Different processes for protein extraction could produce whey protein products with different protein compositions, such as whey protein concentrate (WPC) and whey protein isolate (WPI) [ 1 , 2 ]. WPI has a high protein content, mainly including bovine serum albumin (BSA), β-lactoglobulin (β-Lg), and α-lactalbumin (α-La).…”

Section: Introductionmentioning

confidence: 99%

Surface Hydrophobicity and Functional Properties of Citric Acid Cross-Linked Whey Protein Isolate: The Impact of pH and Concentration of Citric Acid

Wang

et al. 2018

Molecules

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The effects of citric acid-mediated cross-linking under non-acidic conditions on the surface hydrophobicity, solubility, emulsifying, and foaming properties of whey protein isolate (WPI) were investigated. In this research, citric acid-mediated cross-linking could not only increase the surface hydrophobicity of whey proteins at pH 7.0 and 8.0, but it also improved its emulsifying and foaming properties. The emulsifying activity and foaming ability of WPI reached a maximum under the condition of 1% citric acid and pH 7.0. However, the solubility of WPI-CA gradually decreased with pH and the content of citric acid increased. Therefore, the cross-linking mediated by citric acid under non-acidic aqueous conditions, markedly altered the surface hydrophobicity and enhanced emulsifying and foaming properties of WPI.

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Section: Introductionmentioning

confidence: 99%

Surface Hydrophobicity and Functional Properties of Citric Acid Cross-Linked Whey Protein Isolate: The Impact of pH and Concentration of Citric Acid

Wang

et al. 2018

Molecules

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“…These may result from the speed increment in the transitions between the folded and denatured states, 4,5 or from the opening of folding pathways which are energetically unaccessible at room pressure. 6 On the other hand, there are also several practical applications of pressure in the fields of pharmacology, 7 food industry, 8,9 or even medicine, 10 since high pressures can inhibit protein aggregation 11 related to the development of neurodegenerative diseases such as Alzheimer or Parkinson. 12,13 The pressure-temperature behavior for the stability of folded proteins has been known for some years, and has an ela) E-mail: jsbach@quim.ucm.es.…”

Section: Introductionmentioning

confidence: 99%

Simulating protein unfolding under pressure with a coarse-grained model

Perezzan

Rey

2012

The Journal of Chemical Physics

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We describe and test a coarse-grained molecular model for the simulation of the effects of pressure on the folding/unfolding transition of proteins. The model is a structure-based one, which takes into account the desolvation barrier for the formation of the native contacts. The pressure is taken into account in a qualitative, mean field approach, acting on the parameters describing the native stabilizing interactions. The model has been tested by simulating the thermodynamic and structural behavior of protein GB1 with a parallel tempering Monte Carlo algorithm. At low effective pressures, the model reproduces the standard two-state thermal transition between the native and denatured states. However, at large pressures a new state appears. Its structural characteristics have been analyzed, showing that it corresponds to a swollen version of the native structure. This swollen state is at equilibrium with the native state at low temperatures, but gradually transforms into the thermally denatured state as temperature is increased. Therefore, our model predicts a downhill transition between the swollen and the denatured states. The analysis of the model permits us to obtain a phase diagram for the pressure-temperature behavior of the simulated system, which is compatible with the known elliptical shape of this diagram for real proteins.

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“…Hence, although these intermediates (between native and fully denatured structures) have an unclear nature, their formation through controlled unfolding of the protein using mild processing could lead to molecules with optimum functional properties (Qi et al, 2001). The potential for food applications could be enormous, especially for proteins not fully exploited at the moment like whey proteins (Liu et al, 2009). High pressure protein structural effects Like for temperature, the pressure effect depends on physicochemical parameters such as the protein concentration, ionic strength, pH, and temperature.…”

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confidence: 99%

High pressure control of protein structure and functionality

Aouzelleg

2014

Nutrition &Amp; Food Science

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Purpose -This article aims to consider the use of high pressure processing in order to gain functional advantages through proteins structure control. High pressure processing has been used to produce high-quality food with extended shelf life and could also be used to modify foods functionality. Design/methodology/approach -The effect of high pressure on protein structure and functionality is looked at and comparisons are made with heat effect in places. b-lactoglobulin and whey proteins are mainly taken as examples.Findings -A controlled partial protein unfolding through mild high pressure processing could lead to a range of intermediate molecular structures. These are distinct from the native and completely unfolded structure and have been referred to as molten globules. The partly unfolded molecular states, hence, are postulated to have increased functionality and could be interesting for the food industry. Originality/value -The opportunity and challenges represented by these theoretical elements are discussed. In particular, the effect of protein concentration and aggregation is emphasised.

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Changes in structure and functional properties of whey proteins induced by high hydrostatic pressure: A review

Cited by 7 publications

References 60 publications

Surface Hydrophobicity and Functional Properties of Citric Acid Cross-Linked Whey Protein Isolate: The Impact of pH and Concentration of Citric Acid

Surface Hydrophobicity and Functional Properties of Citric Acid Cross-Linked Whey Protein Isolate: The Impact of pH and Concentration of Citric Acid

Simulating protein unfolding under pressure with a coarse-grained model

High pressure control of protein structure and functionality

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