2022
DOI: 10.1002/btpr.3232
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Understanding the interaction of proteins to ion exchange chromatographic supports: A surface energetics approach

Abstract: Ion exchange chromatography is one of the most widely used chromatographic technique for the separation and purification of important biological molecules. Due to its wide applicability in separation processes, a targeted approach is required to suggest the effective binding conditions during ion exchange chromatography. A surface energetics approach was used to study the interaction of proteins to different types of ion exchange chromatographic beads. The basic parameters used in this approach are derived fro… Show more

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Cited by 3 publications
(7 citation statements)
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“…Like all polyelectrolytes, lipases at pH values far from their pI are likely to be immobilized by ion exchange on ionic support surfaces of an opposite charge to that of the enzymatic surface; however, the presence of Z potentials (ζ) of an opposite sign on the surface of the support and on that of the protein would be more determinant for the immobilization process, since this potential additionally depends on the ionic strength of the medium. Understanding this mechanism has direct implications for widely used enzyme purification techniques such as ion-exchange chromatography (IEX) [ 163 ]. On the other hand, unlike on hydrophobic surfaces, the orientation of the lipase on the charged exchange support surface will depend on the orientation of its net dipole moment vector: it points towards the surface of the support in the case of an anion exchanger or in the opposite direction in the case of a cation exchanger [ 80 ].…”
Section: Immobilization Of Lipasesmentioning
confidence: 99%
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“…Like all polyelectrolytes, lipases at pH values far from their pI are likely to be immobilized by ion exchange on ionic support surfaces of an opposite charge to that of the enzymatic surface; however, the presence of Z potentials (ζ) of an opposite sign on the surface of the support and on that of the protein would be more determinant for the immobilization process, since this potential additionally depends on the ionic strength of the medium. Understanding this mechanism has direct implications for widely used enzyme purification techniques such as ion-exchange chromatography (IEX) [ 163 ]. On the other hand, unlike on hydrophobic surfaces, the orientation of the lipase on the charged exchange support surface will depend on the orientation of its net dipole moment vector: it points towards the surface of the support in the case of an anion exchanger or in the opposite direction in the case of a cation exchanger [ 80 ].…”
Section: Immobilization Of Lipasesmentioning
confidence: 99%
“…Due to the fact that in this type of immobilization, the interactions are reversible, similar to hydrophobic interactions, they have the potential to facilitate the recovery of the support from a derivative where the lipase has been inactivated. To do this, it is necessary to use solutions with high ionic strength or at a pH that gives the potential lipase (ζ) an equal sign to that of the support [ 163 , 164 ].…”
Section: Immobilization Of Lipasesmentioning
confidence: 99%
“…For a cation exchange process, adsorbent (or stationary phase) consisting of large number of negative charges was required. Highly hydrophilic surface negates the possibility of protein adsorption and any weak cation exchange between the surface and proteins ( [14], [23], [24]). Hence, a suitable copolymer that could adhere to the chromatography column walls was to be chosen without being highly hydrophilic (ca.…”
Section: Surface Morphologymentioning
confidence: 99%
“…b Surface functionalized with ether and(or) hydroxyl groups ([24],[32]) PMMA -poly(methyl methacrylate); ACP -poly(methyl methacrylate-co-methacrylic acid)…”
mentioning
confidence: 99%
“…20,21 b Surface functionalized with ether and(or) hydroxyl groups. 20,21 Sigma, USA). Tetrahydrofuran (THF) was the organic solvent used for ACP dissolution.…”
Section: Introductionmentioning
confidence: 99%