Immobilization of β-glucosidase onto mesoporous silica support: Physical adsorption and covalent binding of enzyme
This paper investigates β-glucosidase immobilization onto mesoporous silica support by physical adsorption and covalent binding. The immobilization was carried out onto micro-size silica aggregates with the average pore size of 29 nm. During physical adsorption the highest yield of immobili...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Serbian Chemical Society
2014-01-01
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| Series: | Journal of the Serbian Chemical Society |
| Subjects: | |
| Online Access: | http://www.doiserbia.nb.rs/img/doi/0352-5139/2014/0352-51391300154I.pdf |
| Summary: | This paper investigates β-glucosidase immobilization onto mesoporous silica
support by physical adsorption and covalent binding. The immobilization was
carried out onto micro-size silica aggregates with the average pore size of
29 nm. During physical adsorption the highest yield of immobilized
β-glucosidase was obtained at initial protein concentration of 0.9 mg ml-1.
Addition of NaCl increased 1.7-fold, while Triton X-100 addition decreased
6-fold yield of adsorption in comparison to the one obtained without any
addition. Covalently bonded β-glucosidase, via glutaraldehyde previously
bonded to silanized silica, had higher yield of immobilized enzyme as well as
higher activity and substrate affinity in comparison to the one physically
adsorbed. Covalent binding did not considerably changed pH and temperature
stability of obtained biocatalyst in range of values that are commonly used
in reactions in comparison to unbounded enzyme. Furthermore, covalent binding
provided biocatalyst which retained over 70% of its activity after 10 cycles
of reuse. [Projekat Ministarstva nauke Republike Srbije, br. III 45021] |
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| ISSN: | 0352-5139 1820-7421 |