Dataset Information

Major Role of Voluminosity in the Compressibility and Sol-Gel Transition of Casein Micelle Dispersions Concentrated at 7 °C and 20 °C.

ABSTRACT: The objective of this work is to bring new information about the influence of temperatures (7 °C and 20 °C) on the equation of state and sol-gel transition behavior of casein micelle dispersions. Casein micelle dispersions have been concentrated and equilibrated at different osmotic pressures using equilibrium dialysis at 7 °C and 20 °C. The osmotic stress technique measured the osmotic pressures of the dispersions over a wide range of concentrations. Rheological properties of concentrated dispersions were then characterized, respectively at 7 °C and at 20 °C. The essential result is that casein micelle dispersions are less compressible at 7 °C than at 20 °C and that concentration of sol-gel transition is lower at 7 °C than at 20 °C, with compressibility defined as the inverse to the resistance to the compression, and that is proportional to the cost to remove water from structure. From our interpretations, these two features were fully consistent with a release of soluble ?-casein and nanoclusters CaP and an increased casein micelle hydration and apparent voluminosity at 7 °C as compared with 20 °C.

SUBMITTER: Doudies F

PROVIDER: S-EPMC6963684 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Publications

Major Role of Voluminosity in the Compressibility and Sol-Gel Transition of Casein Micelle Dispersions Concentrated at 7 °C and 20 °C.

Doudiès Floriane F Arsène Anne-Sophie AS Garnier-Lambrouin Fabienne F Famelart Marie-Hélène MH Bouchoux Antoine A Pignon Frédéric F Gésan-Guiziou Geneviève G

Foods (Basel, Switzerland) 20191206 12

The objective of this work is to bring new information about the influence of temperatures (7 °C and 20 °C) on the equation of state and sol-gel transition behavior of casein micelle dispersions. Casein micelle dispersions have been concentrated and equilibrated at different osmotic pressures using equilibrium dialysis at 7 °C and 20 °C. The osmotic stress technique measured the osmotic pressures of the dispersions over a wide range of concentrations. Rheological properties of concentrated dispe ...[more]

PMID: 31817715

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Project description:Advances in supramolecular assembly have enabled the design and synthesis of functional materials with well-defined structures across multiple length scales. Biopolymer-synthetic hybrid materials can assemble into supramolecular structures with a broad range of structural and functional diversity through precisely controlled noncovalent interactions between subunits. Despite recent progress, there is a need to understand the mechanisms underlying the assembly of biohybrid/synthetic molecular building blocks, which ultimately control the emergent properties of hierarchical assemblies. In this work, we study the concentration-driven self-assembly and gelation of π-conjugated synthetic oligopeptides containing different π-conjugated cores (quaterthiophene and perylene diimide) using a combination of particle tracking microrheology, confocal fluorescence microscopy, optical spectroscopy, and electron microscopy. Our results show that π-conjugated oligopeptides self-assemble into β-sheet-rich fiber-like structures at neutral pH, even in the absence of electrostatic screening of charged residues. A critical fiber formation concentration cfiber and a critical gel concentration cgel are determined for fiber-forming π-conjugated oligopeptides, and the linear viscoelastic moduli (storage modulus G' and loss modulus G″) are determined across a wide range of peptide concentrations. These results suggest that the underlying chemical structure of the synthetic π-conjugated cores greatly influences the self-assembly process, such that oligopeptides appended to π-conjugated cores with greater torsional flexibility tend to form more robust fibers upon increasing peptide concentration compared to oligopeptides with sterically constrained cores. Overall, our work focuses on the molecular assembly of π-conjugated oligopeptides driven by concentration, which is controlled by a combination of enthalpic and entropic interactions between oligopeptide subunits.

Dataset Information

Major Role of Voluminosity in the Compressibility and Sol-Gel Transition of Casein Micelle Dispersions Concentrated at 7 °C and 20 °C.

Publications

Major Role of Voluminosity in the Compressibility and Sol-Gel Transition of Casein Micelle Dispersions Concentrated at 7 °C and 20 °C.

Similar Datasets

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