Correlation between interfacial layer properties and physical stability of food emulsions: current trends, challenges, strategies, and further perspectives.

Whey proteins are globular milk proteins with numerous functional properties and a broad potential for usage in food and supplement-pharmaceutical products. Under various denaturing conditions, whey proteins unfold, form aggregates, microparticles, while at sufficiently high concentrations, gel networks are created. The continuously growing research interest makes it necessary to discuss the recent advances and achievements in this area, including the basic principles of the structural assembly's kinetics along with the different approaches undertaken to fabricate whey protein gels as well as the means to modulate the gel physical properties. This article also focuses on the use of ethanol to modify the structure and functionality of whey proteins, as an alternative way to change the protein conformation and thereby gelation phenomena and functionality.

Whey proteins: Musings on denaturation, aggregate formation and gelation

http://link.springer.com/content/pdf/10.1007/BF03223342.pdf

Whey proteins: Super ingredients for functional foods?

Separation methods for milk proteins on polyacrylamide gel electrophoresis: Critical analysis and options for better resolution

Understanding aggregation in food protein systems is essential to control processes ranging from the stabilization of colloidal dispersions to the formation of macroscopic gels. Patatin rich potato protein isolates (PPI) have promising techno-functionality as alternatives to established proteins from egg white or milk. In this work, the influence of pH and temperature on the kinetics of PPI denaturation and aggregation was investigated as an option for targeted functionalization. At a slightly acidic pH, rates of denaturation and aggregation of the globular patatin in PPI were fast. These aggregates were shown to possess a low amount of disulfide bonds and a high amount of exposed hydrophobic amino acids (S0). Gradually increasing the pH slowed down the rate of denaturation and aggregation and alkaline pH levels led to an increased formation of disulfide bonds within these aggregates, whereas S0 was reduced. Aggregation below denaturation temperature (Td) favored aggregation driven by disulfide bridge formation. Aggregation above Td led to fast unfolding, and initial aggregation was less determined by disulfide bridge formation. Inter-molecular disulfide formation occurred during extended heating times. Blocking different protein interactions revealed that the formation of disulfide bond linked aggregation is preceded by the formation of non-covalent bonds. Overall, the results help to control the kinetics, morphology, and interactions of potato protein aggregation for potential applications in food systems.

https://www.mdpi.com/2304-8158/10/4/796/pdf

Influence of pH, Temperature and Protease Inhibitors on Kinetics and Mechanism of Thermally Induced Aggregation of Potato Proteins

Separation of aggregated β-lactoglobulin with optimised yield in a decanter centrifuge

Selective thermal precipitation followed by a mechanical separation step is a well described method for fractionation of the main whey proteins, α-lactalbumin (α-la) and β-lactoglobulin (β-lg). By choosing appropriate environmental conditions the thermal precipitation of either α-la or β-lg can be induced. Whereas β-lg irreversibly aggregates, the precipitated α-la can be resolubilized by a subsequent adjustment of the solution’s pH and the ionic composition. This study reports on the analytical characterization of resolubilized α-la compared to its native counterpart as a reference in order to assess whether the resolubilized α-la can be considered close to ‘native’. Turbidity and quantification by RP-HPLC of the resolubilized α-la solutions were used as a measure of solubility in aqueous environment. RP-HPLC was also applied to determine the elution time as a measure for protein’s hydrophobicity. DSC measurement was performed to determine the denaturation peak temperature of resolubilized α-la. FTIR spectroscopy provided insights in the secondary structure. The refolding of α-la achieved best results using pH 8.0 and a 3-fold stoichiometric amount of Ca2+ per α-la molecule. The results showed that the mechanism of aggregation induced by gentle thermal treatment under acidic conditions with subsequent mechanical separation is reversible to a certain extent, however, the exact native conformation was not restored.

Molecular Analytical Assessment of Thermally Precipitated α-Lactalbumin after Resolubilization.

Continuous centrifugal separation of selectively precipitated α-lactalbumin

Effect of pH on the reaction mechanism of thermal denaturation and aggregation of bovine β-lactoglobulin

This study investigates the applicability of decanter centrifuges for high efficient separation of valuable proteins from whey. Thus, two different types of protein aggregates, α-lactalbumin (α-la) and β-lactoglobulin (β-lg), were produced by means of selective thermal aggregation. The two aggregate suspensions were investigated for their particle characteristics, sedimentation, and consolidation behavior, and were finally separated in a lab-scale decanter. They showed severe differences in particle size distribution, particle shape, and in the underlying molecular binding mechanisms, all affecting their separability. In scale-down experiments, the non-covalently stabilized α-la aggregates presented sedimentation enhancing flocculation, and a high compressibility of the cake. However, the beneficial sedimentation effects were not observed in the decanter, as the centrifugal forces resulted in particle breakdown. Moreover, the high adhesiveness of sludge-like sediment impeded the discharge. Under best investigated conditions, a clarification around 70% of the supernatant and a dry solid content of 25% in sediment was achieved. Contrary to that, the β-lg aggregates, stabilized by disulfide bonds, were rigid aggregates comprising a median size of 109 μm with irregular shapes. They presented low compressibility in scale-down testing but were discharged as a free-flowing powder from the decanter. The sediment dryness of maximal 40% was attributed to enclosed liquid through thermal aggregation process, which is also reflected in the low particle density. This study demonstrates the successful application of a decanter for the separation of whey proteins and contributes to the understanding of aggregate separability by means of continuous centrifuges.

Separation of Whey Protein Aggregates by Means of Continuous Centrifugation

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