PMID: 11342057May 9, 2001Paper

Homotropic cooperative binding of organic solvent vapors by solid trypsin

Biochimica Et Biophysica Acta
V V GorbatchukB N Solomonov

Abstract

Homotropic cooperative binding was observed at vapor sorption of organic solvents (acetonitrile, propionitrile, ethanol, 1-propanol, 2-propanol, nitroethane) by dried solid trypsin from porcine pancreas (0.05 g H2O/g protein). The vapor sorption isotherms were obtained by the static method of gas chromatographic headspace analysis at 298 K for 'vapor solvent+solid trypsin' systems in the absence of the liquid phase. All isotherms have a sigmoidal shape with significant sorbate uptake only above the threshold of sorbate thermodynamic activity. On the sorption isotherms of non-hydroxylic sorbates the saturation of trypsin by organic solvent was observed above the sorbate threshold activity. The formation of inclusion compounds with phase transition between solvent-free and solvent-saturated trypsin is supposed. Approximation of obtained isotherms by the Hill equation gives the inclusion stoichiometry S, inclusion free energy, and the Hill constant N of clathrates. The inclusion stoichiometry S depends significantly on the size and shape of sorbate molecules and changes from S=31 mol of sorbate per mol of trypsin for ethanol to S=6 for nitroethane. The inclusion free energies determined for the standard states of pure liquid sorba...Continue Reading

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Citations

Mar 6, 2012·Journal of Peptide Science : an Official Publication of the European Peptide Society·Marat A ZiganshinDmitry V Soldatov
May 7, 2011·Journal of Colloid and Interface Science·Alexander V GerasimovJean-Pierre Majoral
Apr 17, 2003·Journal of Agricultural and Food Chemistry·Nikolay A MironovThomas Haertlé
Jul 21, 2006·The Journal of Physical Chemistry. B·Frederic Tewes, Frank Boury

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