Hydroxyapatite-decorated ZrO 2 for α-amylase immobilization: Toward the enhancement of enzyme stability and reusability
Herein, the immobilization of α-amylase onto hydroxyapatite (HA) and hydroxyapatite-decorated ZrO (10%wt) (HA-ZrO ) nanocomposite were investigated. The immobilization yield was 69.7% and 84% respectively. The structural differences were characterized using X-Ray diffraction, attenuated total reflec...
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Veröffentlicht in: | International journal of biological macromolecules 2021-01, Vol.167, p.299 |
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Sprache: | eng |
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Zusammenfassung: | Herein, the immobilization of α-amylase onto hydroxyapatite (HA) and hydroxyapatite-decorated ZrO
(10%wt) (HA-ZrO
) nanocomposite were investigated. The immobilization yield was 69.7% and 84% respectively. The structural differences were characterized using X-Ray diffraction, attenuated total reflectance-Fourier transform infrared spectra, Raman, and scanning electron microscope. After 10 repeated cycles, the residual activity of immobilized α-amylase onto HA and HA-ZrO
nanocomposite was 46% and 70%, respectively. The storage stability was recorded to be 27%, 50% and 69% from its initial activity in the case of free and immobilized enzyme onto HA and HA-ZrO
nanocomposite, respectively after 8 weeks. The pH-activity profile and temperature revealed pH 6.0 and temperature 50 °C as the optimal values of free α-amylase, while the optimum values for α-amylase on HA and HA-ZrO
was shifted to pH 6.5 and 60 °C after immobilization. The immobilized α-amylase onto HA-ZrO
showed comparatively higher catalytic activity than the free α-amylase. The Km value after the immobilization process onto HA was 2.1 folds highly than that of the free enzyme. In conclusion, it can be inferred that HA-ZrO
is more sustainable and beneficial support for enzyme immobilization and it represents promising supports for different uses of α-amylase in the biomedical applications. |
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ISSN: | 1879-0003 |