Viscosity of bovine serum albumin aqueous solutions as a function of temperature and concentration

Monkos, Karol

doi:10.1016/0141-8130(95)01057-2

Cited by 66 publications

(70 citation statements)

References 15 publications

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“…The values of two other parameters are presented in Figure 2. As seen, both S s and D s monotonically increase with increasing concentration and they can be described by the identical equations as E s , but E p and E w should be replaced by ( S p , S w ) and (D p , D w ), respectively [10]. In these relations ( S p , ξ ) and (D p , ξ ) are adjustable parameters.…”

Section: Resultsmentioning

confidence: 99%

“…This may be explained by assuming that the activation energy E s is a superposition of the activation energy of water E w and protein E p molecules. The detailed analysis has shown that this leads to the relation [10]:…”

Section: Resultsmentioning

confidence: 99%

“…Unfortunately, V h for OSA is unknown. However, for several proteins such calculations were made [10,11,13,14] and it was shown that the Simha factor decreases with increasing temperature. At low temperatures, the rotational Brownian motion of proteins -produced as a reaction to the random heat motions of the solvent -is negligible, and all particles should be aligned almost parallel to the direction of flow.…”

Section: Resultsmentioning

confidence: 99%

“…In the present paper, the discussion of the viscosity-temperature relationship of OSA solutions is limited only to the modified Arrhenius formula. It was quite recently successfully applied to several proteins [10][11][12][13][14], and has the form:…”

Section: Resultsmentioning

confidence: 99%

“…To fit the above formula to the experimental values of η and T, the numerical values of S s , D s and E s are needed. For all concentrations, they were calculated by using the least squares method, as described previously [10]. In particular, for water the parameters are as follows: Figure 1 shows the results of such calculations for all measured concentrations.…”

Section: Resultsmentioning

confidence: 99%

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Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

Monkos

2005

J Biol Phys

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Abstract. The influence of protein concentration and temperature on the viscosity of ovine serum albumin (OSA) solutions was studied. The Mooney equation and a modified Arrhenius formula were used to described the viscosity-concentration and viscosity-temperature dependence of the solutions, respectively. The effective specific volume, the activation energy and entropy of viscous flow for hydrated OSA were calculated. The axial ratio and the dimensions of the main semi-axes of hydrated OSA were established. At low concentration limit, the temperature dependence of the intrinsic viscosity and Huggins coefficient is presented. Comparison of some hydrodynamic parameters obtained for different proteins has been made.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

Monkos

2005

J Biol Phys

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Structural interactions of globular proteins—Bovine serum albumin, egg albumin, and lysozyme, in aqueous medium, elucidated with molar volumes, viscosities, energy functions, and IR spectra from 293.15 to 303.15 K

Singh

2006

J of Applied Polymer Sci

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Densities (r), apparent molar volumes (V f ), viscosities (Z), and IR spectra on 0.0010-0.0018% aqueous solutions of bovine serum albumin (BSA), egg albumin (EAlb), and lysozyme at an interval of 0.0004% and at temperatures from 293.15, 298.15, and 303.15 K have obtained. The free energy (DG), entropy (DS), and enthalpy (DH) data with compositions and temperatures are calculated from the values of the flow velocity (v f ) of viscous flow, which decrease with temperature. The densities decrease with concentrations and temperatures except BSA, and the V f values slightly increase with concentrations for BSA and lysozyme, which depict structural reorientations and transition states of protein molecules with increase in viscosities and decrease in reduce viscosities. The reduce viscosities at 293.15 K for BSA, E-Alb, and lysozyme are noted positive, and for BSA and lysozyme remain positive at 298.15 and 303.15 K, whereas for E-Alb it is negative. Activation energies (E*) for lysozyme remain almost constant, and are higher than those of the BSA and E-Alb, respectively, also slightly higher E* values for the BSA than those of the E-Alb at 293.15 and 298.15, and lower than of the E-Alb at 303.15 K, are observed elucidating greater structural interactions for BSA at lower while weaker at temperatures. Stretching frequencies of amide (À ÀNHCOÀ À), À ÀNHÀ À, À ÀCO, and À ÀCHÀ À groups of proteins are noted from IR spectra with broader stretching frequencies for À ÀNHÀ À.

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Rheological properties of collagen/hydroxypropyl methylcellulose (COL/HPMC) blended solutions

Ding

Zhang

2013

J of Applied Polymer Sci

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Collagen/HPMC blends with different HPMC content (HC) were investigated by dynamic responses, creep recovery, thixotropy, and morphological observation. Storage modulus, loss modulus, complex viscosity, and activation energy decreased with the increased HC, while the flow behavior index increased with the increased HC and the dynamic denaturation temperature reached the maximum as HC increased to 50%, indicating that the flowability and thermal stability of collagen solution were improved by the addition of HPMC. However, the blends with higher HC tended to have a relatively lower recovery capacity, and the hysteresis loop areas of the blends were lower than that of collagen (especially when HC > 50%). Additionally, the morphology of collagen/ HPMC was examined by both of atomic force microscopy and scanning electron microscopy. By combining with these results, it seemed that the rheological and structural properties of collagen/HPMC were related to the hydrogen-bond interaction and compatibility between collagen and HPMC molecules.

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Viscosity of bovine serum albumin aqueous solutions as a function of temperature and concentration

Cited by 66 publications

References 15 publications

Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

Determination of Some Hydrodynamic Parameters of Ovine Serum Albumin Solutions Using Viscometric Measurements

Structural interactions of globular proteins—Bovine serum albumin, egg albumin, and lysozyme, in aqueous medium, elucidated with molar volumes, viscosities, energy functions, and IR spectra from 293.15 to 303.15 K

Rheological properties of collagen/hydroxypropyl methylcellulose (COL/HPMC) blended solutions

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