Kinetics of Heat-Induced Aggregation of β-Lactoglobulin

Verheul, Marleen; Roefs, and Sebastianus P. F. M.; Kruif, Kees G. de

doi:10.1021/jf970751t

Cited by 267 publications

(250 citation statements)

References 31 publications

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“…The denatured protein was removed by acid precipitation using an acetic acid buffer pH 4.6 followed by centrifugation at 20,000g for 20 minutes. This is similar to methods employed previously (Verheul et al, 1998). Ju and Kilara (1998) claimed that at pH 4.6 some native whey proteins formed aggregates.…”

Section: Heat Denaturationsupporting

confidence: 87%

The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelation

2007

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The effect of bovine serum albumin (BSA) on the heat induced denaturation, aggregation and subsequent acid-induced gelation of -lactoglobulin (-lg) was investigated in this work. Changes in the denaturation kinetics of -lactoglobulin during heating at 78C were determined by monitoring the disappearance of the native protein by reverse-phase chromatography. Replacing -lactoglobulin with increasing amounts of BSA, while keeping the total protein concentration constant at 5% (w/w), significantly increased the denaturation rate of lactoglobulin from 2.570.30 10 -3 (gL -1 )(1-n)

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Section: Heat Denaturationsupporting

confidence: 87%

The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelation

2007

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“…However, in the pure b-Lg system, a higher proportion of native-like species had disappeared, indicating the contribution of the other proteins to this initial heating phase. The decrease in native-like proteins was reported to be faster when 0.1 mol·L -1 NaCl was added to the b-Lg solution before heating [17,27]. This was not observed in the present work, probably because the high protein concentration by itself promoted the denaturation-aggregation kinetics in samples without added salt.…”

Section: Heat-induced Disappearance Of Native-like B-lg and A -Lacontrasting

confidence: 61%

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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“…According to a few reports, pH value of the extraction bulk was completely dependent on the concentration of acid used. Hence, the modification of the electrostatic interaction and structure of proteins might occur along the changes in acid concentration since pH value was in charge of the charge density of protein [22]. In fact, Wang et al [23] recently stipulated that more positively charged amine groups of collagen were resulted at the pH when the concentration of acetic acid used was at 0.5 M, leading to the highest yield among the studied concentrations.…”

Section: Optimization Of the Psc Extraction Conditionsmentioning

confidence: 99%

Collagen Extraction from Malaysian Cultured Catfish (Hybrid Clarias Sp.): Kinetics and Optimization of Extraction Conditions Using Response Surface Methodology

Kiew

Don

2012

ISRN Chemical Engineering

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A central composite design (CCD) was used for the experimental design and results analysis to obtain the optimal processing parameters (acetic acid concentration, liquid to solid ratio, and stirring speed) for the extraction of pepsin soluble collagen (PSC) from muscles of cultured hybrid catfish of Clarias sp. (Clarias gariepinus ×C. macrocephalus). Statistical analysis showed that the linear and quadratic terms of these three independent variables had significant effects on the yield of PSC. There was also an interaction between the ratio of liquid to solid and the stirring speed in affecting the extraction efficiency. Optimal conditions for a higher yield of PSC were an acetic acid concentration of 0.67 M, a liquid to solid ratio of 24.65 ml/g, and the stirring speed of 423.64 rpm. The verification of the optimization showed that the percentage error differences between the experimental and predicted values were in the range of 0.22-4.42%. The experimental values agreed with the predicted values, indicating an excellent fit of the model used and the success of the response surface methodology in modeling the extraction of PSC from the muscles of catfish. The experimental results were also fitted to the power law model and it was proven to be appropriate in describing the kinetics of collagen extraction process.

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Kinetics of Heat-Induced Aggregation of β-Lactoglobulin

Cited by 267 publications

References 31 publications

The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelation

The influence of bovine serum albumin on β-lactoglobulin denaturation, aggregation and gelation

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

Collagen Extraction from Malaysian Cultured Catfish (Hybrid Clarias Sp.): Kinetics and Optimization of Extraction Conditions Using Response Surface Methodology

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