Complex Between β-Lactoglobulin and κ-Casein. A Review

Sawyer, William H.

doi:10.3168/jds.s0022-0302(69)86753-6

Cited by 191 publications

(110 citation statements)

References 39 publications

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“…Heating unfolds the globular whey proteins and exposes sulphydryl groups, which react with other sulphydryl groups and disulfides and induce linkages and protein-casein aggregates [9,10].…”

Section: Introductionmentioning

confidence: 99%

Influence of dietary fiber addition on some properties of yoghurt

Damian¹

2013

Analele Universitatii "Ovidius" Constanta - Seria Chimie

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The objective of this work was to study the effect of different dietary fibers on rheological properties of yoghurts fortified with these fibers [1,2,3]. Commercial fibers from apple and inulin were used. The effect of addition of dietary fibers in yoghurt [4,5] was investigated by a rotational viscometer, Brookfield viscometer (Brookfield Engineering Inc., Model RV-DV I Prime) with RV spindles. The Brookfield viscometer DV I Prime with disk spindles represents an easy and cheap method for rheological characterization of non-Newtonian fluids, in this case of yoghurt. Syneresis and pH did not show any difference, while only apple fiber yoghurt showed colour differences compared to control.

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“…Heating unfolds the globular whey proteins and exposes sulphydryl groups, which react with other sulphydryl groups and disulfides and induce linkages and protein-casein aggregates [9,10].…”

Section: Introductionmentioning

confidence: 99%

Influence of dietary fiber addition on some properties of yoghurt

Damian¹

2013

Analele Universitatii "Ovidius" Constanta - Seria Chimie

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“…(Fox and McSweeney, 1998) The stability and structure of casein micelles during processing is known to have strong implications on the properties of the final food product. Casein micelle structure has been the focus of exhaustive research (Dalgleish and Parker, 1980, Fox, 1989, Fox and McSweeney, 1998, Horne, 1998, Kruif, 1999, Sawyer, 1969a, Walstra and Jenness, 1984, Waugh and von Hippel, 1956. It is generally accepted that casein micelles exist as roughly spherical, porous entities, 50 nm to 500 nm in diameter, and there are several different models of casein micelle structure.…”

Section: Possible Changes In Casein Micellesmentioning

confidence: 99%

“…The interaction between κ-CN. and β-LG involves both a sulphydryl-disulphide interchange mechanism and non-covalent interaction (Sawyer, 1969b). Interactions between κ-CN.…”

Section: Wheymentioning

confidence: 99%

Effect of sodium chloride addition during diafiltration on the solubility of milk protein concentrate

Gualco¹

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There is considerable interest among food manufacturers to incorporate protein into food products in both developed and developing countries. Dairy proteins are excellent choices for many different applications, as they are known to have several nutritional and functional benefits. Membrane filtration techniques are often utilized as the preferred method of fractionation, due to the high throughput and continuous nature of the process. One such product produced from membrane filtration of skim milk is called milk protein concentrate. This product is valued for its high protein content, but it has historically exhibited poor solubility when reconstituted into water, which severely restricts the food applications for which it is suitable. There is some existing evidence that milk protein concentrates which contain elevated levels of sodium exhibit higher solubility upon reconstitution into water. The main objective of this thesis project was to demonstrate the effect of sodium chloride, added to diafiltration water utilized during the manufacturing process, on the solubility of milk protein concentrate.It was observed that the addition of sodium chloride into diafiltration water at levels of 50 mM, 100 mM, and 150 mM had a beneficial effect on the solubility of milk protein concentrate across a variety of reconstitution conditions. For example, when milk protein concentrate was mixed for 1 h on a stage mixer at 23 °C ± 1 °C, a significant increase (p < 0.001) in mean solubility was observed when at least 50 mM NaCl had been incorporated into DF water. The incorporation of 50 mM NaCl into DF water v significantly increased (p < 0.001) the mean solubility of milk protein concentrate from 59.81 % to between 64.34 % and 71.78 %. The addition of 100 mM NaCl significantly increased (p < 0.001) the solubility to between 88.80 % and 96.24 %, and the addition of 150 mM NaCl significantly increased (p = 0.005) the solubility to between 92.79 % and 100 %.Minerals analysis of dry powders revealed a significant increase (p < 0.001) in levels of sodium. The addition of 50 mM NaCl into DF water was associated with a significant increase (p < 0.001) in powder Na content to between 2.48 mg/g and 7.44 mg/g. The addition of 100 mM NaCl into DF water was associated with a significant increase (p = 0.002) in powder Na content to between 5.80 mg /g and 10.75 mg/g, and the addition of 150 mM NaCl into DF water was associated with a significant increase (p = 0.001) in powder Na content to between 9.57 mg/g and 14.53 mg/g. A significant difference (p < 0.001) in magnesium level was also detected. Differences in calcium content were not found to be statistically significant (p = 0.016) at α = 0.01.Preliminary observations of milk protein concentrate upon reconstitution were made using a confocal laser scanning microscopy method. This method showed evidence of possible differences in powder particle rehydration and affinity for lipid association between powder particles manufactured at different treatment levels. As the level of NaCl incorp...

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“…Mild heat treatments, like thermization (64-68 "C for lOs), have been reported to adequately preserve the renneting properties of raw milk. More severe procedures cause irreversible molecular changes which are related mainly to complex formation via sulphhydryl-disulphide interchange and hydrophobie interactions between~-Iactoglobulin (~-Lg) and x-casein (K-Cn) (Zittle et al, 1962;Sawyer, 1969;Haque and Kinsella, 1988). It seems to be the most important factor affecting the rennet coagulability of heated milk (Van Hooydonk et al, 1987;Dalgleish, 1990).…”

Section: Introductionmentioning

confidence: 99%

Influence of preliminary treatments on structural properties of casein micelles affecting the rennetability

Lieske

1997

Lait

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Summary -Different reconstituted skimmed milk powders, as weil as defatted pasteurized and raw milk, were used to probe the effects of preheating conditions on rennetability and molecular availability of casein to coagulate and to form a curd. The experiments for following coagulation and gel formation were carried out using the formagraph at pH 6.4, 35 "C, and 3.8% total protein. Two new approaches to estimate the surface protein hydrophobicity (SPH) and to quantify the glycosylated and non-glycosylated caseinomacropeptide (CMP) were used to study the molecular state of casein micelles during the primary and secondary phases of renneting. The latter method was supported by ion-exchange fast-protein liquid chromatography (FPLC) using Mono-Q and Mono-S coJumns. Results with raw milk showed that the SPH of native micellar casein is about eight times higher than that of the individual casein components. In processed milks, the range of maximum SPH decreased as the severity of preheating increased. Il was found that a high SPH is correlated with an optimum micellar structure. The latter is progressively lost by association of denatured~-Iactoglobulin (~-Lg) on the micellar surface, especially with the outer part of non-glycosylated K-casein (K-Cn). The extent of association is related to the severity of preliminary milk treatment, which may be measured by a reduced liberation of non-glycosylated CMP.heating / proteolysis / kinetic / caseinomacropeptide / hydrophobicity Résumé -Influence de prétraitements sur la structure des micelles de caséine et son aptitude à la coagulation. Différentes poudres de lait écrémé reconstitué, ainsi que des laits dégraissé pasteurisé et cru, ont été utilisés pour tester l'effet des conditions de préchauffage sur l'aptitude à la coagulation et sur la disponibilité moléculaire de la caséine pour coaguler et pour former un caillé. Les essais pour suivre la coagulation et la formation du gel ont été réalisés à l'aide du Formagraph à pH 6,3, 35 "C et 3,8 % de protéines totales. Deux nouvelles approches, l'une pour estimer l'hyOral communication at the IDF Symposium 'Ripening and Quality of Cheeses', Besançon, France, February 26-28, 1996. 202 B Lieske drophobicité de surface protéique et l'autre pour quantifier le caséinomacropeptide glycosylé et non glycosylé, ont été utilisées pour étudier la forme moléculaire des micelles de caséine au cours des phases primaire et secondaire de la coagulation. La seconde méthode reposait sur l'emploi de la chromatographie d'échange d'ions FPLC utilisant des colonnes Mono-Q et Mono-S. Les résultats obtenus sur lait cru montrent que l'hydrophobicité de surface de la caséine micellaire native est environ huit fois plus élevée que celle des caséines individuelles. Dans les laits traités, le niveau maximal d'hydrophobicité de surface diminuait lorsque la sévérité du préchauffage augmentait. Il a été montré qu'une hydrophobicité de surface élevée est corrélée avec une structure micellaire optimale. Celle-ci est progressivement perdue par association de~-I...

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Complex Between β-Lactoglobulin and κ-Casein. A Review

Cited by 191 publications

References 39 publications

Influence of dietary fiber addition on some properties of yoghurt

Influence of dietary fiber addition on some properties of yoghurt

Effect of sodium chloride addition during diafiltration on the solubility of milk protein concentrate

Influence of preliminary treatments on structural properties of casein micelles affecting the rennetability

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