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|Type:||Artigo de periódico|
|Title:||Microcalorimetric study of sodium n-alkyl sulfate interactions with trypsin at 298 K.|
|Abstract:||systematic study of the interactions of ionic surfactants with protein trypsin in buffer solution pH 3.5, 7.0 and 9.0, ionic strength 10 mM at 298 K was done using the microcalorimetric technique. In this study, anionic surfactant solutions of the sodium n-alkyl sulfates series (C-8, C-10, C-12 and C-14) were used. The enthalpy of interaction (Delta(int)H(0)) shows that the interaction of the surfactants C-8, C-10, C-12 and C-14 with trypsin in the solution pH 3.5 is an endothermic process with the value of Delta(int)H(0) decreasing linearly with increasing carbon chain length, which is attributed to the unfolding of the polypeptide chain. In the solution pH 7.0, we observed the same trend except for C-14 In the solution pH 9.0, from C-10 the enthapy of interaction didn't change with the increasing of the carbon chain length due to unfolding of the polypeptide, We concluded that when trypsin is folded, the enthalpy of interaction shows a linear relationship with the surfactant's hydrophobicity, in agreement with Traube's rule.|
|Editor:||Soc Brasileira Quimica|
|Appears in Collections:||Artigos e Materiais de Revistas Científicas - Unicamp|
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