The influence of temperature- and divalent-cation-mediated aggregation of β-casein on the physical and microstructural properties of β-casein-stabilised emulsions

Li, Meng; O’Mahony, James A.; Kelly, Alan L.; Brodkorb, André

doi:10.1016/j.colsurfb.2019.110620

Cited by 21 publications

(5 citation statements)

References 43 publications

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“…Volume‐weighted average particle size ( D 4,3 ) and ζ‐potential of emulsions were measured using Malvern Zetasizer 3000HSA (MALVERN Instruments). The samples were diluted 1:500 in deionized water to prevent repeated scattering (Li et al., 2020).…”

Section: Methodsmentioning

confidence: 99%

Study on the interaction mechanism of whey protein isolate with phosphatidylcholine: By multispectral methods and molecular docking

Ma,

Wu,

et al. 2024

Journal of Food Science

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The elucidation of the interaction mechanism between phospholipids and milk proteins within emulsions is pivotal for comprehending the properties of infant formula fat globules. In this study, multispectral methods and molecular docking were employed to explore the relationship between phosphatidylcholine (PC) and whey protein isolate (WPI). Observations indicate that the binding constant, alongside thermodynamic parameters, diminishes as temperature ascends, hinting at a predominantly static quenching mechanism. Predominantly, van der Waals forces and hydrogen bonds constitute the core interactions between WPI and PC. This assertion is further substantiated by Fourier transform infrared spectroscopy, which verifies PC's influence on WPI's secondary structure. A detailed assessment of thermodynamic parameters coupled with molecular docking reveals that PC predominantly adheres to specific sites within α‐lactalbumin, β‐lactoglobulin, and bovine serum albumin, propelled by a synergy of hydrophobic interactions, hydrogen bonding, and van der Waals forces, with binding energies noted at −5.59, −6.71, and −7.85 kcal/mol, respectively. An increment in PC concentration is observed to amplify the emulsification properties of WPI whilst concurrently diminishing the zeta potential. This study establishes a theoretical foundation for applying the PC–WPI interaction mechanism in food.

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Section: Methodsmentioning

confidence: 99%

Study on the interaction mechanism of whey protein isolate with phosphatidylcholine: By multispectral methods and molecular docking

Ma,

Wu,

et al. 2024

Journal of Food Science

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“…We would also like to thank Veronica Cueva for her guidance and support, Leslie Howarth for helping design the algorithm for collecting literature/patents from databases, and Kelley J. Donaghy for carefully editing the manuscript. Individual illustrations/images used in Figures 1-4 were reproduced/adapted with permission from the following publishers, whom the authors would also like to thank: Springer Nature (Figure 1 [Rayner et al, 2016]; Figure 2b,d,f-j [Nijenhuis, 1997]; Figure 2u,v [Copetti et al, 1997]; Figure 2w [Tako et al, 2010]), The Royal Society of Chemistry (Figure 1 [Goff & Guob, 2019]; Figure 3i [Patel, Schatteman, De Vosb, & Dewettinck, 2013]; Figure 4a [Leick et al, 2010]; Figure 4d,e [Erramreddy et al, 2017]), The American Chemical Society (Figure 2s,t [Egermayer et al, 2004]; Figure 2x [Paradossi et al, 2002]; Figure 3j [Ju & Kilara, 1998]), The American Physical Society (Figure 3b,d [Terao & Nakayama, 1998]), John Wiley & Sons (Figure 2c [Guenet, 1992]), and Elsevier (Figure 1 [Dickinson, 2012;Eliot et al, 2005]; Figure 2a [Duconseille et al, , 2015], Figure 2e [Arnott et al, 1974]; Figure 2n,o [Yang et al, 2020], Figure 2r [Hansen et al, 2008], Figure 2y [Dea et al, 1977]; Figure 3a [Dickinson, 2015], Figure 3c [Berli et al, 2003], Figure 3e,f [Dickinson, 2012]; Figure 3g [Eliot et al, 2005], Figure 3h [ L...…”

Section: A C K N O W L E D G M E N T Smentioning

confidence: 99%

“…(a) Rheology of gel transition, where Φ m is maximum packing fraction (Dickinson, 2015). Schematic of (b) flocculation (Terao & Nakayama, 1998) and (c) cluster–cluster aggregation (Berli et al., 2003); (d) phase diagram of reversible cluster–cluster aggregation (Terao & Nakayama, 1998); Emulsions can gel via (e) flocculation or (f) gelation of continuous phase (Dickinson, 2012); (g) Schematic (Eliot et al., 2005) and (h) fluorescence image of heat‐induced flocculation of caseinate‐coated O/W emulsion (Li et al., 2020); (i) shellac oleogel (Patel, Schatteman, De Vosb, & Dewettinck, 2013); (j) protein microgel network formation (Ju & Kilara, 1998). For copyright permissions, see ACKNOWLEDGMENTS…”

Section: Thermoreversible Networkmentioning

confidence: 99%

“…Adding salt serves to moderate electrostatic interactions between the adsorbed phosphate groups of the adsorbed casein molecules, such that upon heating, the caseins become dehydrated, which increases hydrophobic interactions between droplets, thus inducing flocculation without any coalescence (Figures 3g,h). This heat‐induced gel can then be reversibly melted upon cooling (Dickinson & Casanova, 1999a; Eliot et al., 2005; Li et al., 2020). Excess salt causes irreversible precipitation, as does too much heat (>50°C).…”

Section: Thermoreversible Networkmentioning

confidence: 99%

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Heat‐ and shear‐reversible networks in food: A review

Kierulf

Whaley²,

Liu³

et al. 2022

Comp Rev Food Sci Food Safe

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While nature behaves like an irreversible network with respect to entropy and time, certain systems in nature exist that are, to some extent, reversible. The property of reversibility imparts unique benefits to systems that possess them, making them suitable for designing self‐healing, stimuli‐responsive, and smart materials that can be used in widely divergent fields. Reversible networks are currently being exploited for applications in tissue engineering, drug delivery, and soft robotics. They are also being utilized as low‐calorie fat mimetics with melt‐in‐your‐mouth textures, as well as being explored as potential scaffolds for three‐dimensional (3D) printable food, among other applications. This review aims to gather representative examples of heat‐ and shear‐reversible networks in the food science literature from the last 30 or so years, in other words, reversible food gels made either from linear biopolymers or from colloidal, particulate dispersions, including those that have been modified specifically to induce reversibility. An overview of the network mechanisms involved that impart reversibility, including a discussion of the strength and range of forces involved, will be highlighted. A model that explains why certain networks are thermoreversible while others are shear‐reversible, and why others are both, will also be proposed. A fundamental understanding of these mechanisms will prove invaluable when designing reversible networks in the future, making possible the precise control of their properties, thus fostering innovative applications within the food industry and beyond.

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“…It consists of a single 209 amino acid chain. The molecule has a versatile and flexible, nonintramolecular cross-linked secondary structure and is an amphiphilic phosphoprotein with a hydrophilic region of negative charged N-terminal and a strongly hydrophobic area at the C-terminus (Li et al, 2020). Two primary variants of β-casein A1 and A2, with at least 10 subvariants, can be classified as β-casein families.…”

Section: β-Caseinmentioning

confidence: 99%

Potential nutraceuticals from the casein fraction of goat’s milk

Dhasmana

Das

Shrivastava

2021

Journal of Food Biochemistry

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Goat is one of the major dairy and meat providers. In terms of structure, nutrient content, and medicinal properties, goat milk is somewhat different from other milk. The differences in composition are important in determining the technical suitability of goat milk and its products for health benefits. In recent years, there has been increasing attention to the identification and molecular composition of milk proteins and the interest in caprine milk. Casein, which accounts for almost 80% of all the proteins, is the most significant protein found in goat milk. It is a pioneer in the field of nutraceutical formulation and drug production by using the goat mammary gland as a bioreactor. In goat milk, the most prevalent proteins are αS‐casein, β‐casein, and κ‐casein. The aim of this review is to highlight the importance of goat milk casein and also focus on recent findings on their medicinal importance that may be helpful for further research on dairy products with health beneficial properties for humans as a remarkable nutraceutical. Practical applications Goat milk casein is considered as a healthy nutrient as well as a therapeutic agent to control abnormal or disease conditions through some of its biologically active peptide residues. Casein fractions of goat milk have been shown to exhibit different biologic activities. Therefore, this study aims to observe the use of goat milk in various disorders and to know about the different products made from goat milk. It will be helpful in the field of medicine to be a new active constituent for the management of various disease conditions.

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The influence of temperature- and divalent-cation-mediated aggregation of β-casein on the physical and microstructural properties of β-casein-stabilised emulsions

Cited by 21 publications

References 43 publications

Study on the interaction mechanism of whey protein isolate with phosphatidylcholine: By multispectral methods and molecular docking

Study on the interaction mechanism of whey protein isolate with phosphatidylcholine: By multispectral methods and molecular docking

Heat‐ and shear‐reversible networks in food: A review

Potential nutraceuticals from the casein fraction of goat’s milk

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