Thermal stability of β-lactoglobulin in the presence of aqueous solution of alcohols and polyols

Romero, Carmen M.; Lozano, José Manuel; Sancho, Javier; Giraldo, Gloria I.

doi:10.1016/j.ijbiomac.2006.10.003

Cited by 33 publications

(17 citation statements)

References 37 publications

(54 reference statements)

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“…Especially interesting are lower alkanediols used on a large scale as chemical intermediates, solvents, and antifreeze; as additives in food, cosmetics, tobacco, and pharmaceutics; as lubricants in the food industry; and as components of operating liquids in refrigerating and thermostatting systems [1]. This group of compounds is also widely used in cryobiology [2] and can be used as protein-stabilizing agents [3,4]. Moreover, lower alkanediols can be treated as specific model substances (which exhibit two donor and two acceptor functions) for much more complicated molecules and macromolecules of biological materials.…”

Section: E Zorębski (B)mentioning

confidence: 99%

The Effect of Pressure and Temperature on the Second-Order Derivatives of the Free Energy Functions for Lower Alkanediols

Zorębski

2014

Int J Thermophys

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The second-order derivatives of the free energy functions, i.e., isochoric molar heat capacities, isentropic and isothermal molar compressibility, and isobaric and isentropic molar thermal expansion, were calculated in the temperature range from (293.15 to 318.15) K and at pressures up to 100 MPa for 1,2-and 1,3-propanediol; 1,2-, 1,3, and 1,4-butanediol; and 2-methyl-2,4-pentanediol. The data for calculations were obtained by means of the acoustic method. The pressure and temperature dependencies for the above mentioned properties are analyzed and discussed together with the literature data on isobaric molar heat capacities. The observed marked difference between isobaric and isentropic thermal expansion is analyzed as well. The differences in behavior of linear 1,2-diols and α, ω-diols as well as a diol with a branched carbon chain are emphasized. The isentropic and isothermal molar compressibilities are used to evaluate the dimensionality and relative rigidity of H-associates.

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Section: E Zorębski (B)mentioning

confidence: 99%

The Effect of Pressure and Temperature on the Second-Order Derivatives of the Free Energy Functions for Lower Alkanediols

Zorębski

2014

Int J Thermophys

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“…In that paper, using hydrogen deuterium (HD) studies monitored by IR spectroscopy, the authors have shown that in presence of sucrose a structurally ordered species of the protein molecule with lower surface area gets populated [18]. Romero et al [19] studied thermal stability of ␤-lactoglobulin in the presence of aqueous solution of alcohols and polyols by fluroscence measurements and their thermodynamic results show that alcohol denaturating effect diminishes gradually as the number of OH groups increase. Thus, the fluorescence studies clearly indicate the difference in the mechanism of stabilization by individual cosolvents.…”

Section: Solventmentioning

confidence: 99%

Mechanism of solvent induced thermal stabilization of papain

Sathish

Kumar

Prakash

2007

International Journal of Biological Macromolecules

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“…Urea enhances the unfolding and exposure of interior protein residues and forms a complex with denatured proteins (Damodaran and others 2007). Alcohols interact favorably with hydrophobic regions of protein molecules, such as β‐lactoglobulin (BLG), that become exposed during heating (Romero and others 2007). Aggregation can be inhibited either by stabilizing proteins against denaturation, or by preventing aggregation of already denatured proteins.…”

Section: Introductionmentioning

confidence: 99%

Ingredients and pH are Key to Clear Beverages that Contain Whey Protein

LaClair

Etzel

2010

Journal of Food Science

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A challenge of shelf stable beverages that contain whey protein is that a small portion of protein can be denatured and aggregated during thermal processing, resulting in a turbid solution or white precipitate that consumers perceive as a defect. In this study, 3 approaches were taken to reduce turbidity in heat-treated beverages that contain whey protein: (1) centrifugation to remove insoluble protein aggregates, (2) addition of ingredients, and (3) alteration of pH in the range from 3.0 to 4.0. At pH 3.6 and below, all samples were essentially clear both before and after heating for all ingredients. At a pH of 3.8 and above, ingredient selection was crucial to solution clarity after heat treatment. At a pH of 4.0, addition of salts at both 10 and 50 mM increased the turbidity significantly compared to the control, which contained only whey protein in water. Neither addition of sugars at 25, 50, and 100 g/L, nor addition of sugar alcohols at 25 g/L significantly affected turbidity after heat treatment compared to the control. However, sugar alcohols added at 50 or 100 g/L significantly reduced turbidity after heat treatment compared to the control. Removal of insoluble protein aggregates by centrifugation prior to heat treatment resulted in a statistically significant decrease in turbidity after heat treatment. Understanding these results at the molecular level will assist food scientists in selecting processing treatments, ingredients, and pH in the development of shelf stable clear beverages that contain whey protein.

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Thermal stability of β-lactoglobulin in the presence of aqueous solution of alcohols and polyols

Cited by 33 publications

References 37 publications

The Effect of Pressure and Temperature on the Second-Order Derivatives of the Free Energy Functions for Lower Alkanediols

The Effect of Pressure and Temperature on the Second-Order Derivatives of the Free Energy Functions for Lower Alkanediols

Mechanism of solvent induced thermal stabilization of papain

Ingredients and pH are Key to Clear Beverages that Contain Whey Protein

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