Conformational state and charge determine the interfacial stabilization process of beta-lactoglobulin at preoccupied interfaces

Schestkowa, Helena; Wollborn, Tobias; Westphal, Alexander; Wagemans, Anja Maria; Fritsching, Udo; Drusch, Stephan

doi:10.1016/j.jcis.2018.10.043

Cited by 41 publications

(16 citation statements)

References 67 publications

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“…The increase in viscosity due to the lowering degree of degradation of the starch conversion products slows the translational motion of the protein to the interface. This motion is affected by LG to the o/w interface with the same equipment [11,37]. This increase of 4 s can be explained with their lower protein injection volume and lower water drop volume which causes less bulk motion.…”

Section: Time Dependent Adsorption Behaviormentioning

confidence: 92%

“…The experiments were performed in triplicate. On the basis of Böttcher, Keppler, and Drusch (2017) and Schestkowa et al (2019) lag time was determined from the injection time point to the start point of decreasing interfacial tension [11,37]. The analysis is influenced by injection induced motion with a low velocity field in the bulk phase.…”

Section: Time Dependent Adsorption Behaviormentioning

confidence: 99%

“…Its interfacial properties were found to depend on several external factors like environmental conditions e.g. pH, temperature and ionic strength [5][6][7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

“…Both methods are typically used to characterize interfacial properties of substances under aqueous, highly diluted conditions (e.g. [10,11,23]). However, it can be reasonably assumed that changes in physical values like bulk viscosity, flow behavior or density will affect the interfacial properties.…”

Section: Introductionmentioning

confidence: 99%

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Interfacial Properties of β-Lactoglobulin at the Oil/Water Interface: Influence of Starch Conversion Products with Varying Dextrose Equivalents

et al. 2020

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In spray dried emulsions, frequently milk proteins are used as interfacial active components and starch conversion products are added as matrix material at high concentrations. To characterize interfacial properties at the oil/water interface by commonly applied methods, low protein, and carbohydrate concentrations from 1 to 2% are usually analyzed. The impact of a higher concentration of starch conversion products was not investigated so far. Therefore, the formation and rheological properties of β-lactoglobulin (β-LG) stabilized films at the oil/water interface were investigated via short and long-time adsorption behavior using pendant drop tensiometry as well as dilatational and interfacial shear rheology. Suitability of the applied methods to the chosen samples with higher concentrations >1–2% was verified by calculation of selected key numbers like capillary number and by detailed reviewing of the results which is summarized further on as key indicators. It is hypothesized, that the increase in concentration via presence of starch conversion products will delay interfacial stabilization as a result of increased bulk viscosity with decreasing degree of degradation (dextrose equivalent) of the starch. Furthermore, this increase in concentration leads to more stable interfacial films due to thermodynamic incompatibility effects between protein and starch conversion products which results in increases of local protein concentration. Key indicators proved a general suitability of applied methods for the evaluation of the investigated samples. Moreover, results showed an increase in interfacial film stability and elastic properties alongside a decreased interfacial tension if starch conversion products were present in a high concentration.

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Section: Time Dependent Adsorption Behaviormentioning

confidence: 92%

Section: Time Dependent Adsorption Behaviormentioning

confidence: 99%

“…Its interfacial properties were found to depend on several external factors like environmental conditions e.g. pH, temperature and ionic strength [5][6][7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Interfacial Properties of β-Lactoglobulin at the Oil/Water Interface: Influence of Starch Conversion Products with Varying Dextrose Equivalents

et al. 2020

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“…Combined with the more hydrophobic phenolic ring, an amphiphilic molecular structure of the phenolic compound may result. Regarding the interfacial stabilization, factors including the partitioning of the constituents within the dispersed system, the impact of molecular interactions on the adsorption onto the interface, and the changes in interfacial film properties over time as reflected by dilatational rheology should be taken into consideration for a systematic approach [33,34].…”

Section: Introductionmentioning

confidence: 99%

Partitioning Behavior and Interfacial Activity of Phenolic Acid Derivatives and their Impact on β-Lactoglobulin at the Oil-Water Interface

2021

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Proteins are able to stabilize dispersed food systems due to their amphiphilic nature, acting as emulsifiers. Their interfacial properties can be influenced by different methods, including the formation of protein-phenol nanocomplexes. In this study, the interfacial behavior of phenolic compounds and protein-phenol nanocomplexes was first characterized according to the oil-water partitioning behavior of phenolic acid derivatives according to their molecular structure and its impact on interfacial tension. The influence of the phenolic compounds on protein film formation and its properties by dilatational rheology was then evaluated. The most phenolic acid derivatives are predominantly present in the aqueous phase. Despite their hydrophobic benzene body, weak interfacial activity was observed depending on their chemical structure. This result supports possible protein-phenol nanocomplex formation in the aqueous phase and possible interactions at the oil-water interface. Protein-phenol nanocomplexes showed decreased interfacial adsorption properties and decreased viscoelastic interfacial behavior, depending on the expansion of the delocalized π-electrons in the phenol.

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Impact of the Mechanical Stress and Stress Residence Time on Proteins in Emulsion Formulation Within the Premix Membrane Emulsification

Heyse,

Giefer,

Bäther

et al. 2024

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

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Conformational state and charge determine the interfacial stabilization process of beta-lactoglobulin at preoccupied interfaces

Cited by 41 publications

References 67 publications

Interfacial Properties of β-Lactoglobulin at the Oil/Water Interface: Influence of Starch Conversion Products with Varying Dextrose Equivalents

Interfacial Properties of β-Lactoglobulin at the Oil/Water Interface: Influence of Starch Conversion Products with Varying Dextrose Equivalents

Partitioning Behavior and Interfacial Activity of Phenolic Acid Derivatives and their Impact on β-Lactoglobulin at the Oil-Water Interface

Impact of the Mechanical Stress and Stress Residence Time on Proteins in Emulsion Formulation Within the Premix Membrane Emulsification

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