Molecular Mass Distributions of Heat-Induced β-Lactoglobulin Aggregates

Hoffmann, Marion; Sala, Guido; Olieman, C.; Kruif, C. G. de

doi:10.1021/jf9700788

Cited by 102 publications

(95 citation statements)

References 21 publications

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“…It must be noted, however, that a possible urea-induced dissociation of high molecular weight aggregates into smaller ones cannot be excluded. It is possible, as previously suggested by Hoffman et al [14], that some disulphide linked aggregates had formed larger ones via noncovalent interactions. On the other hand, our results suggest that even if noncovalently linked aggregates were formed at a high proportion, they were rapidly converted into disulphide bonded aggregates.…”

Section: Nature Of Stabilising Forces Involved In Formed Aggregatessupporting

confidence: 54%

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Mineral modulation of thermal aggregation and gelation of whey proteins: from ?-lactoglobulin model system to whey protein isolate

Caussin

Famelart

Maubois

et al. 2003

Lait

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-Solutions of 100 g·kg -1 of b-lactoglobulin (b-Lg), b-Lg + a-lactalbumin (a-La), b-Lg + a-La + bovine serum albumin (BSA) or whey protein isolate (WPI) were heated at 75°C, pH 6.8 in water and in the presence of either 100 mmol·L -1 NaCl or 10 mmol·L -1 CaCl 2 . The subsequent polymerisation-aggregation processes in solution before gelation and the physical properties of the formed gels were determined. The disappearance of native-like proteins, formation of b-Lg covalent dimer and the nature of the interactions involved in the formed aggregates were addressed. Whatever the protein system, both NaCl and CaCl 2 increased gel strength and decreased gelation time. At gelling time, relatively small aggregates, formed by the contribution of the total initial amount of proteins, were observed in samples without added salts. In contrast, with NaCl or CaCl 2 , only part of the initial amount of proteins was aggregated before gel time. Very large aggregates were formed in the presence of calcium. Under these two mineral conditions, as well as in samples without added salt, covalent disulphide bonds were seen to be the major forces involved in the aggregation process at gel time.Whey protein / aggregation / gelation / calcium / sodium Résumé -Modulation de l'agrégation et de la gélification des protéines de lactosérum par les minéraux : de la b-lactoglobuline pure à l'isolat de protéines sériques. Des gels de différentes solutions de protéines (b-lactoglobuline (b-Lg), b-Lg + a-lactalbumine (a-La), b-Lg + a-La + sérum albumine bovine (BSA), isolat de protéines sériques) à 100 g·kg -1 étaient formés à pH 6.8 dans l'eau ou dans 100 mmol·L -1 NaCl ou 10 mmol·L -1 CaCl 2 . Les propriétés physiques des gels ainsi que les réactions d'agrégation des protéines (disparition des protéines natives, formation de dimères covalents de b-Lg et nature des liaisons entre protéines agrégées) ont été étudiées. Le NaCl et le CaCl 2 augmentent la force des gels et diminuent les temps de gel (tg). Au tg, sans ajout de sels, les agrégats formés, de petites tailles, impliquent la totalité des protéines présentes en solution. En revanche, en présence de NaCl ou de CaCl 2 , seule une partie des protéines est impliquée dans la formation des agrégats au tg. La taille des agrégats formés est plus élevée en présence de CaCl 2 . Dans toutes les conditions, les ponts disulfures interprotéiques semblent être les liaisons majoritairement impliquées dans la formation des agrégats au tg.Protéine de lactosérum / agrégation / gélification / calcium / sodium * Corresponding author: sbouhal@rennes.inra.fr 2 F. Caussin et al.

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Section: Nature Of Stabilising Forces Involved In Formed Aggregatessupporting

confidence: 54%

“…Hoffmann et al [14] showed that noncovalent interactions are of minor importance in the formation of b-Lg aggregates after heating at neutral pH and 65°C. They postulated the prominent role of disulphide bonds.…”

Section: Nature Of Stabilising Forces Involved In Formed Aggregatesmentioning

confidence: 99%

Mineral modulation of thermal aggregation and gelation of whey proteins: from ?-lactoglobulin model system to whey protein isolate

Caussin

Famelart

Maubois

et al. 2003

Lait

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“…4,9,10 The heat-induced denaturation and aggregation are also affected by pH and ionic environment of the medium. 11,12 For valueadded industrial applications of WP, the composition and the changes in both the physico-chemical and functional properties need to be accurately analyzed.…”

Section: Introductionmentioning

confidence: 99%

Comparison of Size-Exclusion Chromatography and Flow Field-Flow Fractionation for Separation of Whey Proteins

Kang¹,

Moon²,

Lee³

2011

Bulletin of the Korean Chemical Society

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Whey protein (WP) is a mixture of proteins, and is of high nutritional values. WP has become an important source of functional ingredients in various health-promoting foods. In this study, size-exclusion chromatography (SEC) and asymmetrical flow field-flow fractionation (AsFlFFF) were used for separation and analysis of whey proteins. It was found that a lab-prepared WP from raw milk is mostly of β-lactoglobulin with small amount of higher molecular weight components, while a commercial whey protein isolate (WPI) powder contains relatively larger amount of components other than β-lactoglobulin, including IgG and protein aggregates. Results suggest that AsFlFFF provides higher resolution for the major whey proteins than SEC in their normal operation conditions. AsFlFFF could differentiate the BSA and Albumin, despite a small difference in their molecular weights, and also was able to separate much smaller amount of aggregates from monomers. It is noted that SEC was able to show the presence of low molecular weight components other than the major whey proteins in the WP samples, which AsFlFFF could not show, probably due to the partial loss of those low molecular weight species through the membrane.

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“…Each monomer has a molecular weight of 18.3 kDa, contains 162 amino acid residues, two disulphide bonds (C106-C119 and C66-C160) and one free cysteine residue (C121) [6][7][8] . Upon heating, betalactoglobulin dissociates into monomers, leading to exposure of hydrophobic groups and the free sulfhydryl group [9,10] . This then gives rise to aggregation and/or polymerization [4,5,9,11,12] .…”

Section: Introductionmentioning

confidence: 99%

“…Upon heating, betalactoglobulin dissociates into monomers, leading to exposure of hydrophobic groups and the free sulfhydryl group [9,10] . This then gives rise to aggregation and/or polymerization [4,5,9,11,12] . Beta-lactoglobulin is sensitive to heating at 60-100°C.…”

Section: Introductionmentioning

confidence: 99%

The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin

Ghahghaei¹

2008

American J. of Biochemistry and Biotechnology

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Aggregation of beta-lactoglobulin occurs mainly via intermolecular disulphide bond exchange. Upon heating, beta-lactoglobulin aggregated which increased with increasing pH. The presence of DTT led to more rapid aggregation and precipitation of beta-lactoglobulin. AlphaCrystallin prevented the aggregation of heat-stressed beta-lactoglobulin and was a more efficient chaperone at higher pH values. In the presence of DTT, however, alpha-crystallin was a less efficient chaperone due to faster aggregation of heated and reduced beta-lactoglobulin.

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Molecular Mass Distributions of Heat-Induced β-Lactoglobulin Aggregates

Cited by 102 publications

References 21 publications

Mineral modulation of thermal aggregation and gelation of whey proteins: from ?-lactoglobulin model system to whey protein isolate

Mineral modulation of thermal aggregation and gelation of whey proteins: from ?-lactoglobulin model system to whey protein isolate

Comparison of Size-Exclusion Chromatography and Flow Field-Flow Fractionation for Separation of Whey Proteins

The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin

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