Adsorption of β-Lactoglobulin on Thiol-Functionalized Mesoporous Silica

被引:2
|
作者
Chaabane, Laroussi [3 ]
Loupiac, Camille [3 ]
Bouyer, Frederic [1 ]
Bezverkhyy, Igor [1 ]
Foley, Sarah [2 ]
Assifaoui, Ali [3 ,4 ]
机构
[1] Univ Bourgogne, Lab Interdisciplinaire Carnot Bourgogne, UMR 6303, CNRS, F-21078 Dijon, France
[2] Univ Bourgogne Franche Comte, Lab Chrono Environm, UMR CNRS 6249, F-25000 Besancon, France
[3] Univ Bourgogne Franche Comte, Univ Bourgogne, Inst Agro, INRAE,UMR PAM 1517, F-21000 Dijon, France
[4] Univ Bourgogne, Sch Pharm, Dept Pharmaceut Technol, F-21079 Dijon, France
关键词
ENZYME IMMOBILIZATION; SBA-15; ADSORBENT; REMOVAL; NANOPARTICLES; IONS; SEPARATION; PROTEINS; DYES;
D O I
10.1021/acs.langmuir.4c01099
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
SBA-15 mesoporous materials were synthesized with different pore sizes (5 and 10 nm) and thiol-functionalized groups and then characterized to describe their ability to differentially adsorb beta-lactoglobulin (BLG), a globular protein with an ellipsoid shape measuring 6.9 nm in length and 3.6 nm in width. All adsorption experiments showed that the adsorption capacities of mesoporous materials for BLG were dependent on the duration of contact between the two materials (mesoporous material and BLG) and the initial BLG concentration. It was also shown that the pore sizes and thiol groups of SBA-15-based adsorbents are important factors for the BLG adsorption capacities. Among the tested adsorbents, thiol-functionalized SBA-15 with a 10 nm pore size (SBA-15-SH-10) showed the highest adsorption capacity (0.560 g<middle dot>g(-1)) under optimal experimental conditions. Kinetics studies demonstrated that the adsorption occurs predominantly inside the pores, with interactions occurring on heterogeneous surfaces. In addition, the thermodynamic parameters indicate a spontaneous and exothermic behavior of the BLG adsorption process onto the thiol-functionalized SBA-15 mesoporous adsorbent. Finally, the characterization of the SBA-15-SH-10 adsorbent at 308 K showed the occurrence of an oxidation reaction of the thiol groups to sulfonate groups during the adsorption process as confirmed by Raman spectroscopy. The spectra recorded after adsorption of the protein showed that this adsorption did not affect the secondary structure of the protein.
引用
收藏
页码:16132 / 16144
页数:13
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