Formation and properties of the whey protein/κ-casein complexes in heated skim milk – A review

Donato, Laurence; Guyomarc’H, Fanny

doi:10.1051/dst:2008033

Cited by 229 publications

(165 citation statements)

References 163 publications

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“…It is known that heat processing of cream modifies the composition and structure of MFGM to a considerable extent [8,24]. Heat treatment denatures whey and MFGM proteins, resulting in the formation of various complexes with caseins [3,5,8,29]. These heat-induced interactions are likely to modify the bioactivity and functional properties of MFGM.…”

Section: Introductionmentioning

confidence: 99%

Effect of cream pasteurization, microfiltration and enzymatic proteolysis on in vitro cholesterol-lowering activity of buttermilk solids

Conway

Gauthier

Pouliot

2010

Dairy Sci. Technol.

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-The lipids and proteins of buttermilk solids have been associated with several potential health benefits. In this work, the effect of cream pasteurization, microfiltration (MF) and enzymatic proteolysis on the chemical composition and cholesterol-lowering activity of buttermilk solids was studied. Buttermilk was made from pasteurized or unpasteurized cream and fractionated using a 0.5-μm MF membrane or treated with pepsin or pepsin followed by trypsin. The cholesterollowering activity of the products obtained was measured as micellar solubility of cholesterol in vitro. This value was reduced significantly by 57.1% of the control in the presence of raw-cream buttermilk, while buttermilk from pasteurized cream had a much lower impact (reduction of 17.0%). These results suggest a strong inhibitory effect of components in raw-cream buttermilk on in vitro micellar solubility of cholesterol. MF retentate and permeate of buttermilks made from either cream had smaller effects on micellar solubility. Enzymatic hydrolysis of buttermilk made from pasteurized cream seemed to restore the lost cholesterol-lowering activity.buttermilk / milk fat globule membrane / pasteurization / microfiltration / cholesterol-lowering activity / enzymatic hydrolysisRésumé -Effet de la pasteurisation de la crème, du fractionnement par microfiltration et de la protéolyse enzymatique sur l'activité hypocholestérolémiante in vitro des solides du babeurre. Les lipides et protéines du babeurre sont associés à différentes activités biologiques bénéfiques pour la santé. Le but de cette étude était de mesurer l'effet de la pasteurisation de la Article published by EDP Sciences crème, de la microfiltration (MF) et de la protéolyse enzymatique sur la composition chimique et l'activité anti-cholestérol des solides du babeurre. Des babeurres issus de crèmes crues ou pasteurisées ont été fractionnés à l'aide d'une membrane de 0,5 μm ou hydrolysés à l'aide de pepsine ou de pepsine suivie de trypsine. L'activité hypocholestérolémiante des produits ainsi obtenus a été mesurée en termes de solubilité micellaire du cholestérol in vitro. Une réduction de 57,1 % par rapport au témoin a été obtenue en présence du babeurre issu de crèmes crues, tandis que l'impact du babeurre issu de crèmes pasteurisées était plus faible (réduction de 17,0 %). Ces résultats suggèrent la présence, dans le babeurre issu de crèmes crues, de composants inhibant fortement la solubilité micellaire du cholestérol in vitro. Les rétentats et perméats des babeurres issus des crèmes crues ou pasteurisées ont eu des effets moins importants sur la solubilité micellaire du cholestérol. L'hydrolyse enzymatique du babeurre issu de crèmes pasteurisées a permis de rétablir, au moins en partie, l'activité hypocholestérolémiante perdue. babeurre / membrane de globule de gras / pasteurisation / microfiltration / activité hypocholestérolémiante / hydrolyse enzymatique

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Section: Introductionmentioning

confidence: 99%

Effect of cream pasteurization, microfiltration and enzymatic proteolysis on in vitro cholesterol-lowering activity of buttermilk solids

Conway

Gauthier

Pouliot

2010

Dairy Sci. Technol.

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“…3). This result indicates that the formation of the aggregates could result from the formation of intermolecular disulfide bonds between denatured Lf, like the formation of the protein-protein complexes observed in heated skim milk (Brisson et al 2007b;Donato and Guyomarc'h 2009). In other words, the higher-level structure of denatured Lf could change, forming soluble aggregates.…”

Section: Discussionmentioning

confidence: 87%

Native, but not thermally denatured lactoferrin solubilizes iron in the presence of bicarbonate ions

Ueno

Kato

Ueda

et al. 2011

Dairy Science & Technol.

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Lactoferrin (Lf) can solubilize more than a 70-fold molar equivalent of iron in the presence of bicarbonate anions. Iron solubilized by Lf (FeLf) is a useful food product for iron fortification, preventing anaemia with no risk of toxicity. However, the mechanism underlying this iron solubilization is not yet well understood. The objective of this study was to investigate the effects of thermal treatments on the iron-solubilizing capacity of Lf in the presence of sodium bicarbonate. Lf was subjected to thermal treatment at 50-80°C for 10 min, and the Lf heated to over 70°C was precipitated by the addition of Fe(III). No precipitation was observed in FeLf-like mixtures of heated Lf when various other cations were substituted for Fe(III): Cu(II), Zn(II), Mg or Na. The precipitation was related to the degree of thermal denaturation of Lf, accompanied by the formation of high-molecular-weight aggregates as disulphide bonds were established. Transferrin, α-lactalbumin and β-lactoglobulin did not solubilize Fe(III), suggesting that the Fe(III)-solubilizing capacity is characteristic of Lf. In conclusion, native Lf is responsible for iron solubilization in the presence of bicarbonate anions. Owing to the application of native Lf to the manufacture of FeLf, FeLf can improve specific food products by supplementing their iron content.

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“…Heating milk at temperatures above ~60°C for 5-10 min induces the unfolding and assembling of the whey proteins into aggregates (WPA) of 0.1 µm size through thiol-disulfide and hydrophobic interactions [6]. Meanwhile, heating pure whey protein systems or whey products produces aggregates of diameter > 1 µm [7][8][9].…”

Section: Introductionmentioning

confidence: 99%

New insight on the formation of whey protein microbeads by a microfluidic system

Andoyo

Guyomarc’H

Tabuteau

et al. 2018

AIP Conference Proceedings

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Abstract. The current paper describes the formation of whey protein microbeads (WPM) having a spherical shape and a monodispersed size distribution. A microfluidic flow-focusing geometry was used to control the production of whey protein microdroplets in a hydrophobic phase. The microfluidic system consists of two inlet channels where the WPI solution and the lipophilic phase were separately injected towards the flow-focusing (FF) junction where they eventually meet, then co-flow. A whey protein isolate (WPI) solution of 150 g/kg protein and two types of hydrophobic phases, i.e. sunflower oil and n-dodecane, were tested as the continuous phase. The formation of WPM was observed microscopically. The aim of the present study was to describe the production of stable monodisperse WPM in suspension in milk ultrafiltrate using a microfluidic system. Hints to perform the control of the running parameters, i.e. choice of the hydrophobic phase or fluids flowrates, are provided. The results showed that in the sunflower oil, microdroplets had a large polydisperse size distribution, while in n-dodecane, microdroplets with narrow size distribution were obtained. Stabilization of the whey protein microdroplets through heat-gelation at 75 °C for 20 min in n-dodecane produced WPM and no change in shape nor size is observed. Meanwhile replacing the n-dodecane by MUF using centrifugation and washing caused the swelling of the WPM, but dispersity remained low. From this study, microfluidic system seemed to be a suitable method to be used for producing small quantities of monodisperse WPM.

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Formation and properties of the whey protein/κ-casein complexes in heated skim milk – A review

Cited by 229 publications

References 163 publications

Effect of cream pasteurization, microfiltration and enzymatic proteolysis on in vitro cholesterol-lowering activity of buttermilk solids

Effect of cream pasteurization, microfiltration and enzymatic proteolysis on in vitro cholesterol-lowering activity of buttermilk solids

Native, but not thermally denatured lactoferrin solubilizes iron in the presence of bicarbonate ions

New insight on the formation of whey protein microbeads by a microfluidic system

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