Coupling population balance model and residence time distribution for pilot-scale modelling of β-lactoglobulin aggregation process

Erabit, Nicolas; Ndoye, Fatou-Toutie; Álvarez, G.; Flick, Denis

doi:10.1016/j.jfoodeng.2015.12.013

Cited by 7 publications

(7 citation statements)

References 34 publications

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“…It is easy to control aggregate size at laboratory scale, but Erabit et al (2014), working with microgel aggregates, already showed that the control of aggregate size with physicochemical parameters was more difficult under dynamic conditions because of the contribution of shear forces. Several authors have studied the impact of temperature, shear or flow regime on whey protein aggregate size (Erabit et al, 2016;Kerche et al, 2016;Mahmoudi et al, 2014;Simmons et al, 2007;Wolz et al, 2016) but only few authors have produced fractal aggregates at the pilote scale under continuous conditions involving variations of flow regimes and heating residence times (Buggy et al, 2018;Mahmoudi et al, 2014;Nicorescu et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Flow process and heating conditions modulate the characteristics of whey protein aggregates.

Guibert

Hennetier

Martin

et al. 2020

Journal of Food Engineering

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Whey protein fractal aggregates reveal different texturizing properties depending on their size. This study characterize the effect of three process parameters (flow regime, heating residence time (RT h) and heating temperature) on the size and shape of aggregates formed at a semi-industrial scale using a dynamic tubular heat exchanger, and identify the mechanisms involved in their formation. The study showed that physicochemical parameters are not the unique levers to modulate agregates properties but process parameters are also efficient. Asymetrical-Flow-Field-Flow-Fractionation was used to highlight the significant increase of aggregate size produced under transient regime conditions compared to laminar and turbulent regimes. Even larger aggregates were obtained while increasing the heating temperature from 80 to 85°C since the unfolding aggregation of protein was controlled by the aggregation step. Moreover, RT h showed no effect on aggregate formation. This study paves the way to the control of aggregate properties obtained in a continuous dynamic mode.

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Section: Introductionmentioning

confidence: 99%

Flow process and heating conditions modulate the characteristics of whey protein aggregates.

Guibert

Hennetier

Martin

et al. 2020

Journal of Food Engineering

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“…However, for industrial applications, scientific research using whey protein concentrates and whey protein isolates (WPI) at high concentrations are applicable, as these ingredients are similar to the types of ingredients used in the manufacture of infant formula and nutritional beverage products. Previous work has also been carried out, albeit less extensively, using pilot-scale heating equipment, typically in the heat treatment of skim milk (Corredig and Dalgleish, 1996;Oldfield et al, 1998), and to a lesser extent, whey protein concentrates and WPI (Petit et al, 2013;Erabit et al, 2016). Studying the behavior of whey proteins under relevant processing conditions is fundamental to the understanding and optimization of the variables required for the production of stable and viable whey protein products.…”

Section: Introductionmentioning

confidence: 99%

Pilot-scale formation of whey protein aggregates determine the stability of heat-treated whey protein solutions—Effect of pH and protein concentration

Buggy

McManus

Brodkorb

et al. 2018

Journal of Dairy Science

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Denaturation and consequent aggregation in whey protein solutions is critical to product functionality during processing. Solutions of whey protein isolate (WPI) prepared at 1, 4, 8, and 12% (wt/wt) and pH 6.2, 6.7, or 7.2 were subjected to heat treatment (85°C × 30 s) using a pilot-scale heat exchanger. The effects of heat treatment on whey protein denaturation and aggregation were determined by chromatography, particle size, turbidity, and rheological analyses. The influence of pH and WPI concentration during heat treatment on the thermal stability of the resulting dispersions was also investigated. Whey protein isolate solutions heated at pH 6.2 were more extensively denatured, had a greater proportion of insoluble aggregates, higher particle size and turbidity, and were significantly less heat-stable than equivalent samples prepared at pH 6.7 and 7.2. The effects of WPI concentration on denaturation/aggregation behavior were more apparent at higher pH where the stabilizing effects of charge repulsion became increasingly influential. Solutions containing 12% (wt/ wt) WPI had significantly higher apparent viscosities, at each pH, compared with lower protein concentrations, with solutions prepared at pH 6.2 forming a gel. Smaller average particle size and a higher proportion of soluble aggregates in WPI solutions, pre-heated at pH 6.7 and 7.2, resulted in improved thermal stability on subsequent heating. Higher pH during secondary heating also increased thermal stability. This study offers insight into the interactive effects of pH and whey protein concentration during pilot-scale processing and demonstrates how protein functionality can be controlled through manipulation of these factors.

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“…The order of the reaction n is defined as dC agg /dt = kC n nat , where k is the reaction rate constant, which is supposed to be a function of temperature and solvent composition. Reaction orders n were reported to vary between 1 and 2 (Dannenberg & Kessler, 1988;De Wit, 1990;Erabit et al, 2016;Wolz et al, 2016;Roefs & De Kruif, 1994;Phan-Xuan et al, 2011;Zuniga et al, 2010). From kinetic models of β-lactoglobulin that recognized that the rate of nucleation (initiation) is much smaller than the rate of propagation (aggregation), we expected a n of 1.5 (Roefs & De Kruif, 1994;Tolkach & Kulozik, 2007).…”

Section: Kinetics Of Aggregation In Isothermal Conditionsmentioning

confidence: 99%

“…An optimum could exist (Simmons et al, 2007;Wolz et al, 2016). However, this picture is not clearly established for thermal denaturation of proteins due to the difficulty of uncoupling thermal history from flow conditions (Erabit et al, 2016;de Guibert et al, 2020). We studied a range of shear ratesγ which extended from 50 s −1 to 2.66×10 3 s −1 (Fig.…”

Section: Effect Of Shear Ratementioning

confidence: 99%

Kinetic and structural characterization of whey protein aggregation in a millifluidic continuous process

et al. 2021

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Whey protein isolates (WPI) can be aggregated upon heating to create new functional properties (e.g. texture), which depend on aggregate size and structural properties. In industrial conditions, aggregates are obtained in continuous processes at high temperature (≥ 75 • C) in few minutes. When studying the kinetics of WPI aggregation at high temperature and under flow, one major issue is to develop a process in which heat transfer does not limit aggregation. To this end, we used a down-scaling approach in which a WPI solution flows in a heated capillary tube. We show that this process makes it possible to study both the kinetics of aggregation after few seconds and its dependence with the mean shear rate in isothermal conditions. The size and mass of aggregates and protein conformation were characterized by small-angle X-ray scattering and resonant mass measurement for a single physico-chemical condition (pH 7.0, 10 mM NaCl, 92 • C, 4 % w/w WPI) which led to sub-micrometric aggregates. Firstly, we report that the size of aggregates were three times larger than when produced in a test tube. Secondly, the size and mass of aggregates reached a steady-state value in a few seconds, whereas the kinetics of aggregation and denaturation had a characteristic time of few minutes. Thirdly, the shear rate had no significant effect on the size of the aggregates, or on the aggregation kinetics. We concluded that WPI aggregation at 92 • C is limited by a step of nucleation, and that the fact that aggregates produced in test tube were smaller is due to a slower thermalization.

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Coupling population balance model and residence time distribution for pilot-scale modelling of β-lactoglobulin aggregation process

Cited by 7 publications

References 34 publications

Flow process and heating conditions modulate the characteristics of whey protein aggregates.

Flow process and heating conditions modulate the characteristics of whey protein aggregates.

Pilot-scale formation of whey protein aggregates determine the stability of heat-treated whey protein solutions—Effect of pH and protein concentration

Kinetic and structural characterization of whey protein aggregation in a millifluidic continuous process

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