Effect of Meso vs Macro Size of Hierarchical Porous Silica on the Adsorption and Activity of Immobilized β-Galactosidase
β-Galactosidase (β-Gal) is one of the most important enzymes used in milk processing for improving their nutritional quality and digestibility. Herein, β-Gal has been entrapped into a meso-macroporous material (average pore size 9 and 200 nm, respectively) prepared by a sol-gel method from a silica...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1999. - 33(2017), 13 vom: 04. Apr., Seite 3333-3340 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2017
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Enzymes, Immobilized Silicon Dioxide 7631-86-9 beta-Galactosidase EC 3.2.1.23 |
| Zusammenfassung: | β-Galactosidase (β-Gal) is one of the most important enzymes used in milk processing for improving their nutritional quality and digestibility. Herein, β-Gal has been entrapped into a meso-macroporous material (average pore size 9 and 200 nm, respectively) prepared by a sol-gel method from a silica precursor and a dispersion of solid lipid nanoparticles in a micelle phase. The physisorption of the enzyme depends on the concentration of the feed solution and on the pore size of the support. The enzyme is preferentially adsorbed either in mesopores or in macropores, depending on its initial concentration. Moreover, this selective adsorption, arising from the oligomeric complexation of the enzyme (monomer/dimer/tetramer), has an effect on the catalytic activity of the material. Indeed, the enzyme encapsulated in macropores is more active than the enzyme immobilized in mesopores. Designed materials containing β-Gal are of particular interest for food applications and potentially extended to bioconversion, bioremediation, or biosensing when coupling the designed support with other enzymes |
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| Beschreibung: | Date Completed 24.09.2018 Date Revised 24.09.2018 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.7b00134 |