Conditions limiting the influence of thiol–disulphide interchange reactions on the heat-induced aggregation kinetics of β-lactoglobulin

Mounsey, John S.; O’Kennedy, B. T.

doi:10.1016/j.idairyj.2006.12.008

Cited by 41 publications

(30 citation statements)

References 27 publications

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“…However, many authors reported different results when reaction orders were determined experimentally; in general values between first order and second order have been reported depending on the conditions used 5,6,11,23,24 . The mean reaction orders of pure β-lactoglobulin and β-lactoglobulin in WPI were 1.4 under the conditions used here.…”

Section: Discussionmentioning

confidence: 99%

Formation of Non-Native β-Lactoglobulin during Heat-Induced Denaturation

et al. 2011

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Section: Discussionmentioning

confidence: 99%

Formation of Non-Native β-Lactoglobulin during Heat-Induced Denaturation

et al. 2011

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“…The aggregation rate of β -lactoglobulin at 78 ° C at pH 7.0 in water increased 31 times with increasing protein concentrations from 1% to 6% with second -order kinetics. 250 On the other hand, aggregation of GCSF above 2.5 mg/mL at pH 7.0 at 37 ° C follows apparent fi rst -order kinetics, as the rate -limiting step involves a unimolecular process. 18 Similarly, the rate -controlling step in the aggregation of rFVIII is also a unimolecular reaction involving protein conformation changes, leading to fi rst -order aggregation kinetics under thermal stress.…”

Section: Enhanced Protein Aggregation At High Concentrationsmentioning

confidence: 99%

“…For example, binding of calcium to β -lactoglobulin reduced the zeta potential of the protein to a minimum of − 5 mV, accelerating aggregation at pH 7.0. 250 Metal ions can also act at the level of intermolecular interactions critical for the formation of multimeric aggregates. 255 Different metal ions may have different degrees of effect on the same proteins.…”

Section: Metal Ionsmentioning

confidence: 99%

“…The heat -induced aggregation of β -lactoglobulin at pH 7.0 at 78 ° C follows second -order kinetics, but stoichiometric addition of calcium leads to fi rst -order aggregation kinetics. 250 Simmons et al 259 studied the infl uences of temperature (70 -90 ° C) and shear rate (111 -625/s) upon the rate of growth and size of aggregates in whey protein concentrate solutions (WPC35), and the addition of minerals resulted in the formation of much smaller aggre- 255 gates and increased deposition onto the surface of the Couette apparatus. This was attributed to interactions between Ca and β -lactoglobulin both in the bulk and at the heated surface.…”

Section: Metal Ionsmentioning

confidence: 99%

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External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

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The behavior of biotherapeutic proteins is signifi cantly different from small molecule drugs both in liquid and solid states, especially in terms of physical stability. One such property is the high tendency of protein molecules to aggregate under a variety of conditions. The aggregation tendency is arguably the most common and troubling manifestation of protein instability during the development of protein biotherapeutics. 1 Protein aggregates usually exhibit either reduced or, in many cases, no biological activity. 2 -5 A clear correlation was established between loss of recombinant factor VIII (rFVIII ) and its degree of aggregation as shown in Fig. 4.1 . 6 To achieve effective prevention or inhibition of protein aggregation, it is of paramount importance to understand all the possible factors that affect or control the protein aggregation process.Many factors have been identifi ed and reported in the literature affecting the process and rate of protein aggregation. These factors can be roughly divided into two major categories: internal (protein structure related) and external (protein environment related). Chapter 3 in this book has focused extensively on factors that belong to the fi rst category. This chapter focuses on the external factors that affect the process and rate of protein aggregation. To facilitate discussion, these external factors are further divided into the following sections: (1) temperature; (2) solution conditions and composition (pH, buffer type and concentration, ionic strength, excipients and level, protein concentration, metal ions, denaturing and reducing agents, impurities, organic solvents, containers/closures, sources of proteins, sample treatment, and analytical methodologies); (3) processing steps (fermentation/expression,

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“…An increase in the tensile strength observed at 520 kHz for WPC indicates that high-frequency ultrasound may have increased the disulfide linkage in the WPC film. However, the heating effect due to the sonication may also be the reason for the slight increase in the tensile strength: heat-induced aggregation/crosslinking is commonly observed in dairy proteins [68].…”

Section: Modification Of Functional Properties Of Dairy Ingredientsmentioning

confidence: 99%

The ultrasonic processing of dairy products – An overview

Ashokkumar

Bhaskaracharya

Kentish

et al. 2009

Dairy Sci. Technol.

164

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-Ultrasonic processing is an emerging technology in food processing. When ultrasound passes through a liquid, bubble nuclei present in the liquid grow by bubble coalescence and rectified diffusion. When these bubbles reach a critical size range, they collapse under nearadiabatic conditions generating extreme conditions within the bubbles and in the surrounding liquid that include intense shear forces, turbulence and microstreaming effects. These ultrasound-induced physical effects are finding increasing use in food and dairy processing, in applications such as the enhancement of whey ultrafiltration, extraction of functional foods, reduction of product viscosity, homogenization of milk fat globules, crystallization of ice and lactose and the cutting of cheese blocks. After a brief introduction to the ultrasonic processing of food systems in general, this review presents a critical discussion of applications in dairy processing, together with the findings of some recent research on the use of ultrasound to modify the functionality of dairy protein ingredients. ultrasonic processing / acoustic cavitation / whey protein / dairy product Article published by EDP Sciences l'industrie alimentaire et laitière, dans des applications telles que l'amélioration de l'ultrafiltration du lactosérum, l'extraction d'aliments fonctionnels, la réduction de la viscosité des produits, l'homogénéisation des globules gras du lait, la cristallisation de la glace et du lactose et le décou-page des blocs de fromage. Après une brève introduction sur le traitement par ultrasons des systèmes alimentaires en général, cette revue présente une discussion critique des applications en technologie laitière, ainsi que les résultats de certaines recherches récentes sur l'usage des ultrasons pour modifier les fonctionnalités des ingrédients protéiques laitiers.ultrason / cavitation acoustique / protéine de lactosérum / produit laitier

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Conditions limiting the influence of thiol–disulphide interchange reactions on the heat-induced aggregation kinetics of β-lactoglobulin

Cited by 41 publications

References 27 publications

Formation of Non-Native β-Lactoglobulin during Heat-Induced Denaturation

Formation of Non-Native β-Lactoglobulin during Heat-Induced Denaturation

External Factors Affecting Protein Aggregation

The ultrasonic processing of dairy products – An overview

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