Thermal denaturation and heat-induced gelation properties of β-lactoglobulin. Effects of some chemical parameters

Liu, Tong Xun; Relkin, Perla; Launay, B.

doi:10.1016/0040-6031(94)80104-5

Cited by 41 publications

(32 citation statements)

References 30 publications

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“…Thermal stability of several proteins of interest to the food industry were investigated indeed by DSC as affected by various environmental factors. Studies on egg proteins such as ovalbumin [8,9], conalbumin [10] and lyzozyme [11], milk proteins such as beta-lactoglobulin [12][13][14], ot-lactalbumin [15,16] and casein, as well as muscle proteins such as myosin and actin [17,18] and plant proteins such as vicilin from faba beans [8] and rapeseed storage protein [19], and globulins isolated from various cereal grains [20] can be mentioned.…”

Section: Protein Thermal Stability and Denaturationmentioning

confidence: 99%

Application of differential scanning calorimetry in food research and food quality assurance

Fárkas¹,

Mohácsi-Farkas²

1996

Journal of Thermal Analysis

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Differential scanning calorimetry (DSC) is the most widely used thermal analytical technique in food research and it has a great utility in quality assurance of food. Proteins are the most studied food components by thermal analysis including studies on conformation changes of food proteins as affected by various environmental factors, thermal denaturation of tissue proteins, food enzymes and enzyme praparations for the food industry, as well as effects of various additives on their thermal properties. Freezing-induced denaturation of food proteins and the effect of cryoprotectants are also monitored by DSC. Polymer characterization based on DSC of polysaccharides, gelatinization behaviour of starches and interaction of starch with other fbod components can be determined, and phase transitions during baking processes can be studied by DSC. Studies on crystallization and melting behaviour of fats observed by DSC indicate changes in lipid composition or help characterizing products. Thermal oxidative decomposition of edible oils examined by DSC can be used for predicting oil stability. Using DSC in the freezing range has a great potential for measuring and modelling frozen food thermal properties, and to estimate the state of water in foods and food ingredients. Research in food microbiology utilizes DSC in better understanding thermoadaptive mechanisms or heat killing of food-borne microorganisms. lsothermic mierocalorimetric techniques provide informative data regarding microbial growth and microbial metabolism.

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Section: Protein Thermal Stability and Denaturationmentioning

confidence: 99%

Application of differential scanning calorimetry in food research and food quality assurance

Fárkas¹,

Mohácsi-Farkas²

1996

Journal of Thermal Analysis

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“…It is well known, that denaturation of the globular protein β-Lg is dependent on several environmental factors. Besides the temperature, environmental conditions like protein concentration and pH can affect the denaturation kinetics and the polymerisation behaviour of denatured particles [7,8].…”

Section: Introductionmentioning

confidence: 99%

Thermal pre-treatment of β-Lactoglobulin as a tool to steer enzymatic hydrolysis and control the release of peptides

Leeb

Kulozik

Cheison

2011

Procedia Food Science

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Tryptic hydrolysis of β-Lactoglobulin (β-Lg) has been shown as an excellent way to produce several functional peptides. However enzymatic hydrolysis results in a mixture of numerous different peptides, which is problematic regarding the enrichment of one functional peptide in foods. Therefore, a new approach was investigated to control enzymatic hydrolysis by thermal pre-treatment of the substrate to produce specifically desired peptides. For this a 5% β-Lg solution (w/w) was denatured at 80°C and the influence of the surrounding pH (pH 4.6, 6.8 and 8) on the formed denatured particles was characterised by degree of denaturation (DD) and particle size. The native, as well as the denatured protein was then hydrolysed by trypsin (EC 3.4.21.4) at enzyme optimal conditions (pH 8 and 37°C). Hydrolysis was monitored by degree of hydrolysis (DH) using the pH-stat method and the hydrolysates were analysed by MALDI-TOF-MS/MS after several DHs. It could be demonstrated that the attacked cleavage sites during tryptic hydrolysis of native β-Lg followed no specific order. Denaturation independent of the environmental conditions led to a decrease of the DH during the total hydrolysis. Of special interest was the formation of non-native monomers by thermal denaturation at pH 8 and the subsequent decrease of attacked peptide bonds to only five different cleavage sites after a DH of 1%. This conditions were favorable, due to the release of a slightly heterogeneous hydrolysate, containing the functional peptide f(142-148), with reported ACE-inhibitory activity.

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“…Among caseins (the major protein component of milk) only α s2 -and κ-caseins contain disulfide bonds but no free thiol group. Heating solutions of globular whey proteins at temperatures higher than 75 o C may lead to denaturation [14,38,39,41,44], with consequences on surface hydrophobicity [4,29] and the formation of polymers via a SH/S-S interchange reaction between whey proteins themselves [20,33], and also between caseins and whey proteins [12,26,27]. On the other hand, heating milk in mixture with polysaccharides such as carrageenan, at a temperature higher than that of carrageenan transconformation contributes to associative interactions [32].…”

Section: Introductionmentioning

confidence: 99%

Composition of fat protein layer in complex food emulsions at various weight ratios of casein-to-whey proteins

Sourdet¹,

Relkin²,

Fosseux

et al. 2002

Lait

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-We studied three complex food emulsions which differed only by the weight ratio of casein-to-whey proteins (80:20, 60:40, 0:100). We considered the stability of the fat droplets against aggregation/coalescence, the amount of adsorbed proteins, and the protein composition of the interface. Our results indicated that coalescence was inhibited whatever the protein composition. However, aggregation between fat droplets was observed in the casein-free emulsion (0:100), where the amount of adsorbed proteins at the fat globule surface was the lowest. Quantitative SDS-PAGE experiments showed that preferential adsorption of caseins over globular proteins occurs only in the emulsion based on the intermediate (60:40) casein-to-whey protein ratio. Furthermore, the proportion of adsorbed proteins which were found in polymeric forms seemed to increase with decreasing casein-to-whey protein ratio. The fat globule stability, total fat protein load and proportion of adsorbed protein in the polymeric forms were discussed in terms of adsorption properties of milk proteins at the oil-water interface, in relation to the casein-to-whey protein ratio.Milk protein / emulsion / stability / protein adsorption / disulfide bond Résumé -Composition de la couche protéique adsorbée à la surface des globules gras dans des émulsions alimentaires complexes contenant différents rapports caséine/protéines sériques. Nous avons étudié trois émulsions alimentaires complexes qui ne diffèrent entre elles que par le rapport massique caséine/protéines sériques (80:20 ; 60:40 et 0:100). Cette étude a été réalisée en considérant la stabilité des gouttelettes lipidiques vis-à-vis de l'agrégation/coalescence, la quantité de protéines adsorbées par unité de surface de globule gras et la composition de l'interface. Nos résultats ont montré l'absence de coalescence dans les trois émulsions, et la présence d'agrégats n'a été observée que dans l'émulsion (0:100) ne contenant pas de caséine. Dans ce dernier cas, la quantité de protéines adsorbées à la surface des globules gras est la plus faible. Une étude quantitative par électro-phorèse sur gel de polyacrylamide a indiqué une adsorption préférentielle des caséines par rapport aux protéines sériques dans le cas de l'émulsion préparée à base du ratio intermédiaire (60:40) de caséine/protéines sériques. De plus, la proportion de polymères adsorbés à la surface de globules gras semble augmenter lorsque le rapport massique caséine/protéiques sériques diminue. La stabilité des émulsions, la charge protéique des globules gras et la proportion de polymères adsorbés sont discutées en fonction du rapport caséine/protéines sériques.Protéine laitière / émulsion / stabilité / adsorption des protéines / pont disulfure

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Thermal denaturation and heat-induced gelation properties of β-lactoglobulin. Effects of some chemical parameters

Cited by 41 publications

References 30 publications

Application of differential scanning calorimetry in food research and food quality assurance

Application of differential scanning calorimetry in food research and food quality assurance

Thermal pre-treatment of β-Lactoglobulin as a tool to steer enzymatic hydrolysis and control the release of peptides

Composition of fat protein layer in complex food emulsions at various weight ratios of casein-to-whey proteins

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