scholarly journals Hydrophobic interaction adsorption of whey proteins: Effect of temperature and salt concentration and thermodynamic analysis

2006 ◽  
Vol 844 (1) ◽  
pp. 6-14 ◽  
Author(s):  
R BONOMO ◽  
L MINIM ◽  
J COIMBRA ◽  
R FONTAN ◽  
L MENDESDASILVA ◽  
...  
Keyword(s):  
Thermodynamic Analysis ◽  
Hydrophobic Interaction ◽  
Salt Concentration ◽  
Whey Proteins ◽  
Effect Of Temperature

Effect of temperature on the equilibrium solubility of dimethylolpropionic acid: Measurement, correlation, thermodynamic analysis and solvent selection

2021 ◽  
Vol 328 ◽  
pp. 115462
Author(s):  
Vanee Mohdee ◽  
Katarína Fulajtárová ◽  
Tomáš Soták ◽  
Milan Hronec ◽  
Suphot Phatanasri ◽  
...  
Keyword(s):  
Thermodynamic Analysis ◽  
Effect Of Temperature ◽  
Equilibrium Solubility ◽  
Solvent Selection

scholarly journals Fractionation and recovery of whey proteins by hydrophobic interaction chromatography

2011 ◽  
Vol 879 (7-8) ◽  
pp. 475-479 ◽  
Author(s):  
Maria João Santos ◽  
José A. Teixeira ◽  
Lígia R. Rodrigues
Keyword(s):  
Hydrophobic Interaction ◽  
Whey Proteins ◽  
Hydrophobic Interaction Chromatography

scholarly journals Depicting the Non-Covalent Interaction of Whey Proteins with Galangin or Genistein Using the Multi-Spectroscopic Techniques and Molecular Docking

Foods ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 360 ◽  
Author(s):  
Chun-Min Ma ◽  
Xin-Huai Zhao
Keyword(s):  
Molecular Docking ◽  
Hydrophobic Interaction ◽  
Whey Proteins ◽  
Sodium Dodecyl ◽  
Binding Constants ◽  
Spectroscopic Techniques ◽  
Stereochemical Structure ◽  
Non Covalent Interactions ◽  
Β Lactoglobulin ◽  
Covalent Interactions

The non-covalent interactions between a commercial whey protein isolate (WPI) and two bioactive polyphenols galangin and genistein were studied at pH 6.8 via the multi-spectroscopic assays and molecular docking. When forming these WPI-polyphenol complexes, whey proteins had changed secondary structures while hydrophobic interaction was the major driving force. Detergent sodium dodecyl sulfate destroyed the hydrophobic interaction and thus decreased apparent binding constants of the WPI-polyphenol interactions. Urea led to hydrogen-bonds breakage and protein unfolding, and therefore increased apparent binding constants. Based on the measured apparent thermodynamic parameters like ΔH, ΔS, ΔG, and donor-acceptor distance, galangin with more planar stereochemical structure and random B-ring rotation showed higher affinity for WPI than genistein with location isomerism and twisted stereochemical structure. The molecular docking results disclosed that β-lactoglobulin of higher average hydrophobicity had better affinity for the two polyphenols than α-lactalbumin of lower average hydrophobicity while β-lactoglobulin possessed very similar binding sites to the two polyphenols. It is concluded that polyphenols might have different non-covalent interactions with food proteins, depending on the crucial polyphenol structures and protein hydrophobicity.

Behavior of whey proteins in hydrophobic interaction chromatography

1996 ◽  
Vol 19 (9) ◽  
pp. 521-526 ◽  
Author(s):  
Mercedes de Frutos ◽  
Alejandra Cifuentes ◽  
Jose Carlos Diez-Masa
Keyword(s):  
Hydrophobic Interaction ◽  
Whey Proteins ◽  
Hydrophobic Interaction Chromatography

Hydrophobicity gradient columns for the separation of trypsin inhibitor by hydrophobic interaction chromatography at low salt concentration

2003 ◽  
Vol 986 (1) ◽  
pp. 83-88 ◽  
Author(s):  
Yoshio Kato ◽  
Shigeru Nakatani ◽  
Koji Nakamura ◽  
Takashi Kitamura ◽  
Hiroyuki Moriyama ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Hydrophobic Interaction ◽  
Salt Concentration ◽  
Hydrophobic Interaction Chromatography ◽  
Low Salt

scholarly journals Thermodynamic analysis of the gas parameters distribution under leakage from a closed volume with rigid walls

2019 ◽  
Vol 109 ◽  
pp. 00071
Author(s):  
Serhii Ponomarenko ◽  
Oleksandr Zhevzhyk ◽  
Alex Vuginshteyn ◽  
Oleksandr Lutai
Keyword(s):  
Thermodynamic Analysis ◽  
Thermodynamic System ◽  
Effect Of Temperature ◽  
Closed Volume ◽  
Excessive Pressure ◽  
Gas Leakage ◽  
Parallel Processes ◽  
Average Temperature ◽  
Leakage Coefficient ◽  
Rigid Walls

The work deals with the thermodynamic analysis of the parameters of the gas in a closed volume with rigid walls, during its leakage and heat exchange with the environment. Based on the first law of thermodynamics, the law of Fick and the equation of the gas state, we obtained an equation that characterizes the effect of temperature gradient on the mass gas leakage in parallel processes of leakage and heat transfer. The regularity of the leakage coefficient change, determined by the diffusion coefficient, depending on the mass-average temperature in a closed thermodynamic system, is established. The variation of the leakage coefficient for the corresponding ranges of temperature gradients are shown. The research results can be implemented in the development of techniques and technologies for monitoring the tightness of hollow products under excessive pressure of the gas medium.

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