Impact of different aqueous phases on casein micelles: Kinetics of physicochemical changes under variation of water hardness and diafiltration conditions

Reitmaier, Michael; Barbosa, Beatriz Wardzinski; Sigler, Sebastian; Heidebrecht, Hans-Jürgen; Kulozik, Ulrich

doi:10.1016/j.idairyj.2020.104776

Cited by 13 publications

(8 citation statements)

References 42 publications

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“…The difference in αs 1 -casein and β-casein link density is most pronounced (and significant according to statistical analysis) for the yogurt-like gel. This is probably due to the compositional differences between the yogurt-like gel compared to the other gels, such as the presence of heat-denatured whey proteins, heat-treated fat globules (Sharma & Dalgleish, 1993), and/or differences in ionic strength and mineral content (Famelart et al, 1996;Reitmaier et al, 2020).…”

Section: αS 1 -Caseins and β-Caseins Contribute To The Acid-induced P...mentioning

confidence: 99%

Spatial distribution of αs1-caseins and β-caseins in milk gels acidified with glucono-δ-lactone

et al. 2023

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Section: αS 1 -Caseins and β-Caseins Contribute To The Acid-induced P...mentioning

confidence: 99%

Spatial distribution of αs1-caseins and β-caseins in milk gels acidified with glucono-δ-lactone

et al. 2023

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“…Ultrafiltration of milk in diafiltration mode using deionized water further increased the HCT of the final concentrate possibly due to an increase in pH and reduced ionic strength (Sweetsur and Muir, 1980;Muir and Sweetsur, 1984). However, later studies found that demineralization of milk by excessive diafiltration can lead to changes in casein micelle structure depending on the diafiltration medium (Alexander et al, 2011;Reitmaier et al, 2020), moderate to very poor heat stability of milk protein concentrates (Crowley et al, 2014(Crowley et al, , 2015a, and changes in the functional properties of the reconstituted powders (Crowley et al, 2015b(Crowley et al, , 2018. The need for a heat treatment to obtain high-quality milk protein powders or after reconstitution for high milk protein beverages has led to several studies using the subjective heat stability test for the characterization of milk protein concentrates.…”

Section: Concentration By Membrane Technologymentioning

confidence: 99%

Invited review: Heat stability of milk and concentrated milk: Past, present, and future research objectives

Dumpler

Huppertz

Kulozik

2020

Journal of Dairy Science

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The ability of milk and concentrated milk to withstand a defined heat treatment without noticeable changes such as flocculation of protein is commonly denoted as heat stability. A heat treatment that exceeds the heat stability limit of milk or concentrated milk, which has a much lower heat stability, may result in undesired changes, such as separation of milk fat, grittiness, sediment formation, and phase separation. Most laboratory-scale batch heating methods were developed in the early 20th century to simulate commercial sterilization, and these methods have since been standardized. Heat stability studies have been motivated by different objectives during that time, addressing different processing issues and targets in the framework of available technology, legislation, and consumer demand. Although milk hygiene has improved during the last couple of decades, rendering milk less sensitive to coagulation, different standard methods suffered from poor comparability of results, even when comparing results for the same milk sample, indicating that unknown procedural steps affect heat stability. The prediction of heat stability of concentrated milk from the heat stability results of the corresponding unconcentrated milk for rapid quality testing purposes has been difficult, mainly due to different experimental conditions. The objective of this study is to review literature on heat stability, starting from studies in the early 20th century, to summarize the vast number of studies on compositional aspects of milk affecting heat stability, and to lead the way to the most recent work related to compositional changes in concentrates produced by membrane concentration and fractionation, respectively. Particular attention is paid to early and most recent developments and findings, such as the application of kinetic models to predict and limit protein aggregation to assess and describe heat stability as a temperature-time-total milk solids continuum.

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“…However, these authors used distilled water as a dilution medium during sample preparation, which induces major changes to the serum phase. Casein concentration-dependent alterations of CM are known for this modification of the ionic environment, which may primarily have led to the observed colloidal properties. , …”

Section: Introductionmentioning

confidence: 99%

“…Casein concentration-dependent alterations of CM are known for this modification of the ionic environment, which may primarily have led to the observed colloidal properties. 44,45 Recent studies on MCC involving the effects of different changes in the ionic environment focused on the rehydration properties of spray-dried concentrate powders. 46−48 Although the rehydration behavior is critical for the application of powders, other functional aspects like emulsification, foaming, or gelation capabilities will be crucial for using MCC in different food matrices.…”

Section: Introductionmentioning

confidence: 99%

Colloidal Properties of Casein Micelles at Threefold and Natural Concentrations upon Calcium or Chelator Addition: Implications for Binding of Water and Calcium

Reiter

Reitmaier

Kulozik

2022

ACS Food Sci. Technol.

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Understanding the behavior of casein micelles (CMs) in a concentrated state is of interest for the targeted functionalization of micellar casein concentrates (MCCs). We assessed potential differences in colloidal properties of CM at threefold (MCC) and milk-like concentration (MLC) in response to compositional changes of CM caused by modifications of the ionic environment induced by the addition of CaCl 2 and trisodium citrate (TSC). CMs were therefore analyzed regarding surface charge, particle size distribution, volume fraction, and voluminosity. CMs in MCC showed less pronounced colloidal changes induced by TSC and CaCl 2 than equally treated MLC. New mechanistic insights into structural integration and release of water and calcium in or from the micellar structure relative to the observed colloidal changes could be gained. This study offers a better comprehension of the properties of CM in the concentrated state and options for a more targeted design of their functionalities.

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Impact of different aqueous phases on casein micelles: Kinetics of physicochemical changes under variation of water hardness and diafiltration conditions

Cited by 13 publications

References 42 publications

Spatial distribution of αs1-caseins and β-caseins in milk gels acidified with glucono-δ-lactone

Spatial distribution of αs1-caseins and β-caseins in milk gels acidified with glucono-δ-lactone

Invited review: Heat stability of milk and concentrated milk: Past, present, and future research objectives

Colloidal Properties of Casein Micelles at Threefold and Natural Concentrations upon Calcium or Chelator Addition: Implications for Binding of Water and Calcium

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