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Structural, textural and protein adsorption properties of kaolinite and surface modified kaolinite adsorbents
Abstract The structural, textural and protein adsorption properties of kaolinite from clay sedimentary deposits, metakaolinite obtained by thermal dehydroxylation of kaolinite, and the organic derivative prepared by reacting kaolinite with the silane coupling agent tert-butyldimethylchlorosilane, were studied. The retention capacities for the proteins α-lactalbumin (A-LA), bovine serum albumin (BSA) and β-lactoglobulin (B-LG) and the nature of the interactions responsible for protein binding were studied by adsorption experiments, performed at room temperature and pH5.0. The protein adsorption capacity and the selectivity show a clear dependence on the chemical nature of the adsorbents surface and on the textural properties. Kaolinite behaves as a strong adsorbent for A-LA and BSA, and exhibits a very high affinity for B-LG. Metakaolinite shows good retention capacity for A-LA and B-LG, but does not retain significant amounts of BSA. The adsorption capacity of the organo–kaolinite hybrid considerably increases for BSA and A-LA. FTIR results indicate the absence of hydrogen bonding between the adsorbents surface and the polypeptides. The interactions responsible for protein binding are closely related to the hydrophilic or hydrophobic character of the adsorbent surface and the amino acid composition of the proteins, steric effects also should be considered for the adsorption patterns.
Graphical abstract The interaction of BSA with the sylanol–kaolinite complex Display Omitted
Highlights Kaolinite, a low cost non toxic clay, shows high adsorption capacity and different selectivity for whey proteins. A plausible mechanism for silylation of the kaolinite surface was discussed. Silylation of kaolinite generated important changes in the textural parameters. Modification of the kaolinite surface caused substantial changes in protein retention behavior. By surface modification of clays protein adsorbents with desired selectivity can be obtained.
Structural, textural and protein adsorption properties of kaolinite and surface modified kaolinite adsorbents
Abstract The structural, textural and protein adsorption properties of kaolinite from clay sedimentary deposits, metakaolinite obtained by thermal dehydroxylation of kaolinite, and the organic derivative prepared by reacting kaolinite with the silane coupling agent tert-butyldimethylchlorosilane, were studied. The retention capacities for the proteins α-lactalbumin (A-LA), bovine serum albumin (BSA) and β-lactoglobulin (B-LG) and the nature of the interactions responsible for protein binding were studied by adsorption experiments, performed at room temperature and pH5.0. The protein adsorption capacity and the selectivity show a clear dependence on the chemical nature of the adsorbents surface and on the textural properties. Kaolinite behaves as a strong adsorbent for A-LA and BSA, and exhibits a very high affinity for B-LG. Metakaolinite shows good retention capacity for A-LA and B-LG, but does not retain significant amounts of BSA. The adsorption capacity of the organo–kaolinite hybrid considerably increases for BSA and A-LA. FTIR results indicate the absence of hydrogen bonding between the adsorbents surface and the polypeptides. The interactions responsible for protein binding are closely related to the hydrophilic or hydrophobic character of the adsorbent surface and the amino acid composition of the proteins, steric effects also should be considered for the adsorption patterns.
Graphical abstract The interaction of BSA with the sylanol–kaolinite complex Display Omitted
Highlights Kaolinite, a low cost non toxic clay, shows high adsorption capacity and different selectivity for whey proteins. A plausible mechanism for silylation of the kaolinite surface was discussed. Silylation of kaolinite generated important changes in the textural parameters. Modification of the kaolinite surface caused substantial changes in protein retention behavior. By surface modification of clays protein adsorbents with desired selectivity can be obtained.
Structural, textural and protein adsorption properties of kaolinite and surface modified kaolinite adsorbents
Duarte-Silva, R. (author) / Villa-García, M.A. (author) / Rendueles, M. (author) / Díaz, M. (author)
Applied Clay Science ; 90 ; 73-80
2013-12-22
8 pages
Article (Journal)
Electronic Resource
English
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