Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment

Hong, Youn‐Ho; Creamer, Lawrence K.

doi:10.1016/s0958-6946(02)00030-4

Cited by 95 publications

(83 citation statements)

References 57 publications

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“…Previous studies showed that the irreversible transformation of lac into disulphide-bonded dimers, trimers and non-native forms is faster because of the presence of lg. Formation of  lg:lac disulphide-bonded dimers is also caused by the heat effect (Havea et al, 1998;Hong & Creamer, 2002).…”

Section: Whey Protein Denaturationmentioning

confidence: 99%

Influence of moderate electric fields on gelation of whey protein isolate

et al. 2015

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Proteins are one of the food constituents most affected by heating, and some of the changes involve their unfolding, denaturation and gelation. Ohmic heating has often been claimed to improve the quality of foodstuffs due to its uniform heating and (putative) presence of a moderate electric field (MEF). However, this is still subject to discussion, so it is important to determine the effect of ohmic heating and of its MEF upon food constituents. Hence, the aim of this work was to evaluate the effects of MEF on denaturation, aggregation and viscoelastic properties of whey protein isolate (WPI), and compare them with those obtained via conventional heating under identical treatment conditions (up to 30 min at 85 o C). Results have shown that MEF interferes with whey protein unfolding and aggregation pathways at relatively high temperatures. MEF treatments have resulted in WPI solutions possessing more 8 and 10% of native Lactoglobulin and Lactalbumin, respectively, after 30 s of heating at 85 o C, when compared with a conventional heating method. Protein aggregates from MEF-treated WPI solutions presented a maximum increase in size of 78 nm, whereas conventional heating produced an increase of 86 nm. Unlike in conventional heating, aggregation of whey proteins during MEF was not sufficiently strong to form a true elastic gel network, since decreases in both storage and loss modulus were observed following MEF treatment. Our results suggest that MEF may provide a novel method for production of a whey protein matrix with distinctive gel-forming properties.2

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Section: Whey Protein Denaturationmentioning

confidence: 99%

Influence of moderate electric fields on gelation of whey protein isolate

et al. 2015

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“…The major proteins in these whey protein products are α-lactalbumin (α-La; 20%) and β-lactoglobulin (BLG; 50%) 1 . β-Lactoglobulin is a small water-soluble protein that forms the major component of ruminant milk whey 2 .…”

Section: Introductionmentioning

confidence: 99%

A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr⁺³

Behbehania

Divsalar²,

Saboury

2009

Polish Journal of Chemical Technology

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Thermodynamics of the interaction between Cr3+ with β-lactoglobulin type A (BLG-A) was investigated at pH 7.0 and 37 o C by isothermal titration calorimetry. A new method to follow the effect of Cr 3+ on the stability of BLG-A was introduced. The new solvation model was used to reproduce the enthalpies of BLG-A+ Cr 3+ interactions over the whole range of Cr 3+ concentrations. The solvation parameters recovered from the new equation are attributed to the structural change of BLG-A and its biological activity. The results obtained indicate that there is a set of two identical binding sites for Cr for the first and second binding site, respectively. The enthalpy of binding for one mole of Cr +3 ion to one mole of the binding site on BLG-A (ΔH=104.60 kJ mol -1 ) is obtained.

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“…"solid state studies"; and (2) the second group concerns studies which aimed to determine the effect of these factors on the denaturation, polymerisation and/or aggregation of whey protein systems i.e. "liquid state studies" [10,15,[23][24][25][26].…”

Section: Introductionmentioning

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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-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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Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment

Cited by 95 publications

References 57 publications

Influence of moderate electric fields on gelation of whey protein isolate

Influence of moderate electric fields on gelation of whey protein isolate

A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr⁺³

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

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Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment

Cited by 95 publications

References 57 publications

Influence of moderate electric fields on gelation of whey protein isolate

Influence of moderate electric fields on gelation of whey protein isolate

A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr+3

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

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A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr⁺³