Gelation of proteins from milk

Kruif, Kees G. de; Hoffmann, Marion; Marle, M.E. van; Mil, P.J.J.M. van; Roefs, S.P.F.M.; Verheul, Marleen; Zoon, Nel

doi:10.1039/fd9950100185

Cited by 56 publications

(31 citation statements)

References 18 publications

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“…One way to include this attractive part is the Baxter model (Figure 1.2), (Baxter, 1968) commonly known as the "adhesive hard sphere model". It describes the adhesiveness by using a parameter t, which is related to the depth of the attractive well in the interaction potential while its width is regarded to be infinitely small (de Kruif et al, 1995;Mezzenga & Fischer, 2013). Using the Baxter model it is possible to derive the following expression for the osmotic pressure (Parker, Noel, Brownsey, Laos, & Ring, 2005;Prinsen & Odijk, 2004):…”

Section: Theorymentioning

confidence: 99%

Interactions in protein mixtures. Part I: Second virial coefficients from osmometry

et al. 2016

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Section: Theorymentioning

confidence: 99%

Interactions in protein mixtures. Part I: Second virial coefficients from osmometry

et al. 2016

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“…This model has been applied successfully to various systems having short-ranged attractive forces, including sterically stabilized dispersions (31), surfactant-based microemulsions (32), particles flocculated/gelled by bridging polymers (33,34), aggregating casein micelles (11,35), and flocculated caseincoated emulsion droplets (36). The sticky hard-sphere system has a critical temperature defined by τ c = 0.098 and a critical volume fraction φ c = 0.12.…”

Section: Reversible Aggregation and Gelationmentioning

confidence: 99%

Structure and Rheology of Simulated Gels Formed from Aggregated Colloidal Particles

Dickinson

2000

Journal of Colloid and Interface Science

111

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“…Strong disulfide bonds can form between the protein molecules. The denatured proteins tend to aggregate even at low concentrations to form small particles (nanometer scale) (31)(32)(33)(34).…”

Section: Resultsmentioning

confidence: 99%

Practical implications of the phase‐compositional assessment of lipid‐based food products by time‐domain NMR

Duval

Duynhoven

Bot

2006

J Americ Oil Chem Soc

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The objective of this work is to determine the solid fat content (SFC) of the fat-oil phase in oil-in-water (O/W) emulsions, i.e., the droplet SFC, using transverse relaxation decay deconvolution (TRDD) analysis. The TRDD NMR experiment classifies protein protons as mobile, semimobile, and nonmobile. Hence, protein contributes more or less to the solid content detected by TRDD as a function of pH, protein content, and protein denaturation. By taking into account the protein contribution to the overall solid content, one can estimate the droplet solid content in O/W emulsions. The SFC can then be deduced if one converts the ingredients' mass fraction into ingredients' proton fraction using the ingredients' proton densities.Paper no. J11392 in JAOCS 83, 905-912 (November 2006). KEY WORDS:O/W emulsions, SFC, solid content, transverse relaxation decay deconvolution (TRDD), whey proteins.The key to understanding many functional properties of food products and materials is in the physical state of their ingredients (1). Texture (hardness) and melting behavior of margarine and chocolate, for example, are determined by the phase behavior of their lipid component, i.e., the balance between the solid/liquid state and the effects of crystal polymorphism (1,2). For many cereal materials, the phase composition of the carbohydrate components determines processing and textural properties. The various phases comprise different crystalline starch polymorphs, gel states, mesomorphic phases, and liquid-like dissolved phases (3,4). For the assessment of crystal polymorphism of food materials, one traditionally deploys X-ray diffraction and thermal analysis (mostly DSC) (5). These techniques are unsurpassed in addressing specific phase-compositional details of lipid and carbohydrate materials, such as polymorph identification. However, they mostly fall short when the phase composition of complex foods products needs to be assessed in a quantitative manner. For this purpose, NMR relaxometry currently presents the most powerful option. Strong advantages of NMR over other methods are that it probes molecular mobility of the different phases, and that the obtained signals directly relate to corresponding proton densities. For this purpose, dedicated low-field NMR relaxometers have been designed that are relatively cheap and easily operated by nonexperts. The earliest example of a widespread application within the foods community is the determination of solid fat content (SFC) of lipids by NMR (6). This methodology uses rather crude acquisition and data treatments of the free induction decay (FID). More recent sophisticated NMR line-shape analysis procedures (7-9) were introduced to derive detailed quantitative phase-compositional information on polysaccharides (10,11) and on lipids (12). Even thermal denaturation of proteins (13) was investigated. This type of analysis also can be applied to complex food products (8,9,14,15). In our implementation for lipid-based products, we denoted this approach as transverse relaxation decay deconvolu...

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Gelation of proteins from milk

Cited by 56 publications

References 18 publications

Interactions in protein mixtures. Part I: Second virial coefficients from osmometry

Interactions in protein mixtures. Part I: Second virial coefficients from osmometry

Structure and Rheology of Simulated Gels Formed from Aggregated Colloidal Particles

Practical implications of the phase‐compositional assessment of lipid‐based food products by time‐domain NMR

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