Microcalorimetric studies of the interactions of lysozyme with immobilized metal ions: Effects of ion, pH value, and salt concentration

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Title:	Microcalorimetric studies of the interactions of lysozyme with immobilized metal ions: Effects of ion, pH value, and salt concentration
Authors:	Lin,FY;Chen,WY;Sang,LC
Contributors:	化學工程與材料工程學系
Keywords:	AFFINITY-CHROMATOGRAPHY;HISTIDINE-RESIDUES;PROTEIN ADSORPTION;SURFACE-STRUCTURES;BINDING-PROPERTIES;CYTOCHROME-C;ACID-BASE;CU(II);ADSORBENTS;CAPACITY
Date:	1999
Issue Date:	2010-06-29 17:29:01 (UTC+8)
Publisher:	中央大學
Abstract:	This study extends previous research on the interaction of biomaterials with immobilized Cu(II) by isothermal titration calorimetry (ITC) on Fe(III). The difference of the binding behavior of protein with that of the immobilized metal ions is also discussed. For the immobilized Fe(III), ITC results show that the adsorption enthalpy at a constant pH value decreased as the NaCl concentration increased and also decreased with the pH values at constant NaCl concentrations. The adsorption enthalpy become negative under higher pH values or higher salt concentrations indicating the adsorption process is partly driven by the enthalpy. The enthalpy of lysozyme with Fe(III) is higher than that with Cu(II) implying that the heat required for the dehydration of Cu(II) is lower than for the dehydration of Fe(III) and/or that the heat generated from the formation of the coordination with Cu(II) is higher than with Fe(III). In addition, the comparison of different immobilized metal ions corresponding to the equilibrium binding affinity suggests that the binding force of lysozyme with Cu(II) is higher than with Fe(III). This study presents the chemical differences between the binding affinity and the adsorption enthalpy of lysozyme interacting with the immobilized metal ions. The binding and thermodynamic data presented in this study elucidate the mechanism and process of lysozyme binding with immobilized metal ions. In addition, the thermodynamic characteristic functions provide valuable information enabling a more thorough understanding of protein adsorption at the immobilized metal ion affinity surface. (C) 1999 Academic Press.
Relation:	JOURNAL OF COLLOID AND INTERFACE SCIENCE
Appears in Collections:	[National Central University Department of Chemical & Materials Engineering] journal & Dissertation

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