Kinetics of combined thermal and pressure-induced whey protein denaturation in bovine skim milk

Hinrichs, Jörg; Rademacher, B.

doi:10.1016/j.idairyj.2004.07.014

Cited by 56 publications

(53 citation statements)

References 21 publications

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“…The unusual value of the reaction order estimated for the induced denaturation of both proteins subjected to thermal or pressure treatment has been attributed to a complex reaction mechanism that involves many consecutive and/or concurrent steps [19,20]. This could be ascribed to the dissociation of b-lactoglobulin dimer into monomers and to unfolding of monomers followed by aggregation.…”

Section: Resultsmentioning

confidence: 98%

“…Huppertz et al [30] determined that about 36% of the protein was denatured after treatment of milk at 800 MPa at 20°C for 30 min. Hinrichs and Rademacher [20] reported that about 10% of a-lactalbumin was denatured after treatment of milk at 600 MPa for 30 min at 10°C.…”

Section: Resultsmentioning

confidence: 99%

“…The order of reaction published for the pressure denaturation of b-lactoglobulin ranges between 2 and 3. Anema et al [19] and Hinrichs and Rademacher [20] assumed a reaction order of n = 2 for b-lactoglobulin variants A and B treated in milk and in whey protein solutions, whereas a reaction order of n = 2.5 [21] and n = 3 [22] has been also reported for the denaturation of both protein variants by high-pressure treatment.…”

Section: Resultsmentioning

confidence: 99%

“…Denaturation of individual whey proteins in these works has been determined using electrophoresis [19,20] and reversed-phase high performance liquid chromatography (RP-HPLC) [21,22] after subjected pressure-treated milk or whey protein isolate samples to acid precipitation at pH 4.6, to remove precipitated casein and aggregated whey proteins. The order of reaction determined for the pressure-induced denaturation of b-lactoglobulin was found to range between 2 and 3 [19][20][21][22] and of a-lactalbumin between 2 and 2.5 [20][21][22].…”

Section: Introductionmentioning

confidence: 99%

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Effect of high-pressure treatment on denaturation of bovine β-lactoglobulin and α-lactalbumin

Mazri

Sánchez

Ramos

et al. 2012

Eur Food Res Technol

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The effect of high-pressure treatment on denaturation of b-lactoglobulin and a-lactalbumin in skimmed milk, whey, and phosphate buffer was studied over a pressure range of 450-700 MPa at 20°C. The degree of protein denaturation was measured by the loss of reactivity with their specific antibodies using radial immunodiffusion. The denaturation of b-lactoglobulin increased with the increase of pressure and holding time. Denaturation rate constants of b-lactoglobulin were higher when the protein was treated in skimmed milk than in whey, and in both media higher than in buffer, indicating that the stability of the protein depends on the treatment media. a-Lactalbumin is much more baroresistant than b-lactoglobulin as a low level of denaturation was obtained at all treatments assayed. Denaturation of b-lactoglobulin in the three media was found to follow a reaction order of n = 1.5. A linear relationship was obtained between the logarithm of the rate constants and pressure over the pressure range studied. Activation volumes obtained for the protein treated in milk, whey, and buffer were -17.7 ± 0.5, -24.8 ± 0.4, and -18.9 ± 0.8 mL/mol, respectively, which indicate that under pressure, reactions of volume decrease of b-lactoglobulin are favoured. Kinetic parameters obtained in this work allow calculating the pressure-induced denaturation of b-lactoglobulin on the basis of pressure and holding times applied.

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Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effect of high-pressure treatment on denaturation of bovine β-lactoglobulin and α-lactalbumin

Mazri

Sánchez

Ramos

et al. 2012

Eur Food Res Technol

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“…Higher pressures (above 300 MPa) have irreversible and extensive effects on proteins, including denaturation due to unfolding of monomers, aggregation and formation of gel structures [5]. The extent of high-pressure-induced denaturation of whey proteins increases with treatment time [21,22], treatment temperature [17] and pH [2]. The application of pressure has a disruptive effect on intramolecular hydrophobic and electrostatic interactions.…”

Section: Introductionmentioning

confidence: 99%

Effects of high pressure on functionality of whey protein concentrate and whey protein isolate

Krešić

Lelas

Herceg

et al. 2006

Lait

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-The objective of this study was to evaluate the influence of high-pressure treatments on the solubility, surface hydrophobicity, foaming and emulsifying ability of whey protein concentrate (WPC) and whey protein isolate (WPI). Dispersions of WPC and WPI powders (10% (w/w)) were processed at 300 MPa and 600 MPa, for 5 and 10 min at 40 ± 2°C. Changes in protein solubility were determined as solubility at pH 7.0 and at pH 4.6. Assessment of foaming properties was based on the foam expansion during prolonged whipping, and foam stability. Emulsifying properties were characterised by emulsion stability and emulsifying activity indices. The results show significant (P < 0.05) modification of solubility and surface hydrophobicity with increasing intensity and duration of applied pressure, indicating partial denaturation and aggregation of proteins. It was found that high-pressure treatments significantly (P < 0.05) improved the foaming behaviour of WPI, while the foaming ability of WPC was diminished. However, foams formed with high-pressuretreated WPC and WPI exhibited significantly prolonged stability (P < 0.05) compared with control samples. There was a significant trend of decreasing emulsifying efficiency and emulsifying stability related to the intensity of applied pressure and treatment time for both WPC and WPI. emulsifying properties / foaming properties / high pressure / whey protein concentrate / whey protein isolate / solubility / surface hydrophobicity 摘要 -高压处理对乳清浓缩蛋白和乳清分离蛋白的影响。本文研究了高压处理对乳清浓缩蛋白 (WPC) 和乳清分离蛋白 (WPI) 的溶解性、表面疏水性、发泡性和乳化性的影响。在 40°C 下，乳清浓缩蛋白 (10 %, w/w) 和乳清分离蛋白 (10 %, w/w) 的分散液分别在 300 MPa 和 600 Mpa 下高压处理 5 min 和 10 min。在 pH 7.0 和 pH 4.6 测定了两种蛋白质溶解性的变化。以长时间搅打后形成的泡沫膨胀度和泡沫稳定性来评价蛋白质的发泡性能；根据测定乳液稳定性指数和乳化活性指数评价两种蛋白质的乳化特性。试验结果表明，经过高压长时间的处理后，由于蛋白质发生了部分变性和凝聚作用，使得蛋白质的溶解性和表面疏水性发生了显著的改变 (P < 0.05)。高压处理能够显著地改善 WPI 的发泡性 (P < 0.05)，而 WPC 的泡沫形成能力则降低。然而与对照样品相比，经过高压处理后的 WPC 和 WPI 形成的泡沫稳定性有显著提高 (P < 0.05)。随着处理压力和作用时间的增加，两种蛋白质的乳化性和乳化稳定性均呈下降的趋势。乳化性 / 发泡性 / 高压 / 乳清浓缩蛋白 / 乳清分离蛋白 / 溶解性 / 表面疏水性 * Corresponding author (通讯作者): Greta.Kresic@fthm.hrArticle published by EDP Sciences and available at http://www.edpsciences.org/lait or http://dx

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Computational Fluid Dynamics Applied in High‐Pressure Processing Scale‐Up

Rauh

Delgado

2011

Innovative Food Processing Technologies: Advances in Multiphysics Simulation

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Kinetics of combined thermal and pressure-induced whey protein denaturation in bovine skim milk

Cited by 56 publications

References 21 publications

Effect of high-pressure treatment on denaturation of bovine β-lactoglobulin and α-lactalbumin

Effect of high-pressure treatment on denaturation of bovine β-lactoglobulin and α-lactalbumin

Effects of high pressure on functionality of whey protein concentrate and whey protein isolate

Computational Fluid Dynamics Applied in High‐Pressure Processing Scale‐Up

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