Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study

Boye, Joyce I.; Alli, Inteaz

doi:10.1016/s0963-9969(00)00112-5

Cited by 143 publications

(111 citation statements)

References 35 publications

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“…34) As shown in Table 1, the EW proteins were made less thermally stable when heated in the presence of Psi than in the presence of Fru and Suc; that is, the proteins in the aqueous Psi solution might have been unfolded easily. Consequently, the unfolding of protein upon denaturation might have initiated a cross-linking interaction with Psi which further speeded up the unfolding process.…”

Section: Discussionmentioning

confidence: 99%

Rheological Characteristics of Heat-Induced Custard Pudding Gels with High Antioxidative Activity

Sun

Hayakawa

Jiang

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 99%

Rheological Characteristics of Heat-Induced Custard Pudding Gels with High Antioxidative Activity

Sun

Hayakawa

Jiang

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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“…In the case of β-Lg, the largest observed difference (100 ± 20 o C) was shown to depend on with or without TGase. According to the report of Boye and Alli (2000), the endothermic reaction of α-La and β-Lg was denatured significantly at 62 and ~75 o C, respectively. When 100 mM of NaCl was added to 3.0% whey protein isolate, we noted a degeneration of heat absorption at ~87 o C. The unfolding of proteins affects heat absorption via the disruption of non-covalent or disulfide bonds, while it was degenerated by heat and absorbed heat (Fitzsimons et al, 2007).…”

Section: Degeneration Of Protein and Thermolysis Propertiesmentioning

confidence: 94%

Effect of Transglutaminase Addition on the Physicochemical Properties of Sodium Caseinate and Whey Proteins

Jeong¹,

Hong²

2009

Korean Journal for Food Science of Animal Resources

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In this study, several factors were analyzed in an effort to determine the effects of transglutaminase (TGase) treatment on sodium caseinate (NaCN), α-lactalbumin (α-La), and β-lactoglobulin (β-Lg) polymerization reactions. The results of SDS-PAGE showed that NaCN was slightly hydrolyzed to molecular weights of 50-400 kDa according to activation time. α-La formed high-molecular polymers of 30-300 kDa, whereas β-Lg remained almost completely unhydrolyzed. Melting temperatures of NaCN, α-La with and without TGase were all in the range of 100±10 o C under the endothermic curve, and the melting temperature of β-Lg with TGase was lower than that with TGase. When the proteins were incubated for 3 h with TGase, the micrographic structures showed a small quantity of sediment and broad layers. The final α-La residues remained at a level of 21.38%, and the TGase-treated α-La was confirmed to have undergone a profound loss of mass, to 18.25%. The DPPH-radical scavenging activity of NaCN and β-Lg with TGase treatment was higher than that observed in the untreated sample, while those of α-La increased with concentration.

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“…It has also been reported that added sugars have a greater stabilizing effect on β-lactoglobulin than on α-lactalbumin [9] which could also lead to altered ratios of the two proteins in the aggregates from standardized milks compared to unstandardized milks. However, these studies show the difference between low and much higher levels of lactose.…”

Section: Soluble Aggregate Compositionmentioning

confidence: 99%

Role of protein aggregation in heat-induced heat stability during milk powder manufacture

Williams

D'ath

Zisu

2008

Dairy Sci. Technol.

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-Although the inherent heat stability and the processes leading to the heat-induced coagulation of milk and reconstituted milk powders have been studied extensively, the processes that lead to heat-induced heat stability are less well established. An investigation has been undertaken into the effects of standardization with milk permeate or lactose and the heat-stabilization of milk powders. Standardized and unstandardized milk powders were produced in spring and autumn to determine seasonal effects on their heat stability. Other standardized powders were produced using a range of preheat treatments (85 • C/1800 s, 120 • C/120 s, and 140 • C/5 s) to evaluate the effects of preheat treatment and standardization on the heat stability of milk powders. Micelle size and the soluble aggregates formed during the preheat treatment were characterized by a combination of size-exclusion chromatography and SDS-PAGE. The heat stability of the powders was evaluated in a bench-scale model of retorted recombined evaporated milk manufacture. As has been generally accepted, the heat stability may be mediated by the way in which the milk responds to the preheat treatment given during milk powder manufacture. However, we have found that causing the denaturation of the whey proteins in itself, as is indicated by analytical measures such as the whey protein nitrogen index (WPNI) is not sufficient to impart heat stability. Our work suggests that milks with good heat stability are achieved by heating to give a low WPNI and a balance of moderately sized soluble aggregates and a decrease in the proportion of smaller micelles. The formation of these aggregates is influenced by the heating regime applied and varies at different times of year.heat stability / milk protein aggregation / micellar integrity Résumé -Rôle de l'agrégation des protéines dans la stabilité thermique thermo-induite au cours de la fabrication de poudre de lait. Bien que la stabilité thermique inhérente et les processus conduisant à la coagulation thermo-induite du lait et des poudres de lait reconstituées aient été largement étudiés, les processus qui conduisent à la stabilité thermique thermo-induite sont moins bien établis. Une étude a été entreprise concernant les effets de la standardisation avec du perméat de lait ou du lactose et la stabilisation thermique des poudres de lait. Des poudres de lait, standardisé et non standardisé, ont été produites au printemps et en automne pour déterminer l'effet saison sur leur stabilité thermique. D'autres poudres standardisées ont été produites en appliquant différents prétraitements thermiques (85 • C/1800 s, 120 • C/120 s et 140 • C/5 s) pour évaluer les effets du pré-traitement et de la standardisation sur la stabilité thermique des poudres de lait. La taille des micelles et les agrégats solubles formés au cours du prétraitement thermique ont été caractérisés en combinant chromatographie d'exclusion de taille et électrophorèse SDS-PAGE. La stabilité thermique des poudres était évaluée à l'aide d'un modèle simulant...

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Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study

Cited by 143 publications

References 35 publications

Rheological Characteristics of Heat-Induced Custard Pudding Gels with High Antioxidative Activity

Rheological Characteristics of Heat-Induced Custard Pudding Gels with High Antioxidative Activity

Effect of Transglutaminase Addition on the Physicochemical Properties of Sodium Caseinate and Whey Proteins

Role of protein aggregation in heat-induced heat stability during milk powder manufacture

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