Kinetics of denaturation and aggregation of highly concentrated β-Lactoglobulin under defined thermomechanical treatment

Quevedo, María Cristina Céspedes; Kulozik, Ulrich; Karbstein, Heike P.; Emin, M. Azad

doi:10.1016/j.jfoodeng.2019.109825

Cited by 18 publications

(19 citation statements)

References 48 publications

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“…Increasing the shear rate to 50 s − 1 led to a decrease in the aggregation onset temperature to 66 and 76 °C, for βLG and αLA, respectively. This effect was also observed in our previous studies on WPI and βLG [ 7 , 10 ]. It seems that the aggregation onset temperatures determined for the sheared WPI systems corresponded to the onset temperatures of the single protein fractions.…”

Section: Resultssupporting

confidence: 88%

“…Defined treatments at extrusion-like conditions and inline rheological measurements were performed by a closed cavity rheometer (CCR) (RPA flex, TA Instruments, New Castle, DE, USA) as described in our previous study in detail [ 7 ].…”

Section: Methodsmentioning

confidence: 99%

“…The effect of the heat and shear treatment on the denaturation kinetics was described using formal reaction kinetics. The kinetic parameters were determined using a non-linear regression (NLR) method as described by [ 7 ]. An integrated form of the general reaction rate (Equation (2)) can describe the rate of protein denaturation:

where C 0 and C T are the concentrations (g g −1 ) of native whey proteins before and after treatment, respectively, n is the overall order of the reaction and k is the apparent reaction rate constant ((g g −1 ) (1− n ) s −1 ).…”

Section: Methodsmentioning

confidence: 99%

“…Using the Arrhenius Equation (Equation (3)), the temperature dependence of the reaction rate can be described:

where T is the treatment temperature (K), R is the universal gas constant (8.314 kJ kmol K −1 ), k T,n is thermal-induced rate constant, k 0, T,n pre-exponential factor, and E T,A is the activation energy (kJ mol −1 ). Since additional shear stress is also expected to influence the reaction kinetics of highly concentrated whey protein systems [ 7 ], the modified Arrhenius equation developed from a Boltzmann distribution of mechanical energy in a shear field [ 8 ] (Equation (4)) was used to describe the influence of shear stress on the denaturation reaction kinetics:

where k τ,n is the reaction rate constant for the shear-induced reaction and k τ ,0 is a constant analogous to k 0, T,n in the Arrhenius equation. E τ is shear activation energy, J is the average rate of shear energy input, and the factor a relates J to the average amount of mechanical energy temporarily stored in a mole of chain bonds of the sheared system.…”

Section: Methodsmentioning

confidence: 99%

“…Since a better understanding of the denaturation behavior of proteins subjected to various process conditions can be used to develop process-engineering approaches to design whey proteins with new functionalities, information about the effect of combined thermal and mechanical treatment on the denaturation reaction and kinetics of proteins at protein concentrations above 30% is needed. Accordingly, in our recent study [ 7 ] the influence of protein concentration, treatment temperature, and shear rate on denaturation and aggregation kinetics of β-Lactoglobulin (βLG) as a model protein system at concentrations above 50% ( w/w ) was investigated. The results showed that denaturation and aggregation reaction rates decreased with increasing protein concentration.…”

Section: Introductionmentioning

confidence: 99%

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Denaturation Behavior and Kinetics of Single- and Multi-Component Protein Systems at Extrusion-Like Conditions

Quevedo¹,

Karbstein²,

Emin³

2020

Polymers

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In this study, the influence of defined extrusion-like treatment conditions on the denaturation behavior and kinetics of single- and multi-component protein model systems at a protein concentration of 70% (w/w) was investigated. α-Lactalbumin (αLA) and β-Lactoglobulin (βLG), and whey protein isolate (WPI) were selected as single- and multi-component protein model systems, respectively. To apply defined extrusion-like conditions, treatment temperatures in the range of 60 and 100 °C, shear rates from 0.06 to 50 s⁻1, and treatment times up to 90 s were chosen. While an aggregation onset temperature was determined at approximately 73 °C for WPI systems at a shear rate of 0.06 s⁻1, two significantly different onset temperatures were determined when the shear rate was increased to 25 and 50 s⁻1. These two different onset temperatures could be related to the main fractions present in whey protein (βLG and αLA), suggesting shear-induced phase separation. Application of additional mechanical treatment resulted in an increase in reaction rates for all the investigated systems. Denaturation was found to follow 2.262 and 1.865 order kinetics for αLA and WPI, respectively. The reaction order of WPI might have resulted from a combination of a lower reaction order in the unsheared system (i.e., fractional first order) and higher reaction order for sheared systems, probably due to phase separation, leading to isolated behavior of each fraction at the local level (i.e., fractional second order).

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Section: Resultssupporting

confidence: 88%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…Using the Arrhenius Equation (Equation (3)), the temperature dependence of the reaction rate can be described:

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Denaturation Behavior and Kinetics of Single- and Multi-Component Protein Systems at Extrusion-Like Conditions

Quevedo¹,

Karbstein²,

Emin³

2020

Polymers

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Effects of preheating temperatures on β‐lactoglobulin structure and binding interaction with dihydromyricetin

Zhang

Guan

Huang

et al. 2022

eFood

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Low aqueous solubility limits the bioactivity and bioaccessibility of dihydromyricetin (DHM). Preheating treatment affects the loading efficiency of β-lactoglobulin (β-Lg) to polyphenols, but the mechanism remained unclear. In this study, a serial of temperatures (298 K, 318 K, 338 K, 358 K, and 373 K) were set to analyze the preheating effects on the loading efficiency of β-Lg to DHM, and secondary structure change, binding interactions, and particle size distribution were measured and compared with discover the effects. β-Lg preheated at 358 K possessed the highest binding percentage of 0.45, higher than 0.27, 0.30, 0.36, and 0.40 at 298 K, 318 K, 338 K, and 373 K, the exposure of inside hydrophobic residues contribute the hydrophobic interaction with DHM. Fluorescence quenching and molecular docking analysis showed that DHM tend to bind to β-Lg preheated at 358 K with a binding constant of 1.76 × 10 5 L mol −1 and a binding score of −5.84 kcal mol −1 , higher than that of other temperatures. Particle size distribution showed that Z-average size at 358 K was 16.34 nm, significantly higher than others of 7.64, 8.06, 6.84, and 13.4 nm. Preheating unfolded the structure of β-Lg, exposing the internal residues and enhancing the interaction with DHM.

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Influence of Thermomechanical Stresses on Structural and Functional Changes of Highly Concentrated Protein Systems in Extrusion Processing

Gräfenhahn,

Ellwanger,

Karbstein

et al. 2024

Dispersity, Structure and Phase Changes of Proteins and Bio Agglomerates in Biotechnological Processes

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Kinetics of denaturation and aggregation of highly concentrated β-Lactoglobulin under defined thermomechanical treatment

Cited by 18 publications

References 48 publications

Denaturation Behavior and Kinetics of Single- and Multi-Component Protein Systems at Extrusion-Like Conditions

Denaturation Behavior and Kinetics of Single- and Multi-Component Protein Systems at Extrusion-Like Conditions

Effects of preheating temperatures on β‐lactoglobulin structure and binding interaction with dihydromyricetin

Influence of Thermomechanical Stresses on Structural and Functional Changes of Highly Concentrated Protein Systems in Extrusion Processing

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