Abstract:
:Herein, the immobilization of α-amylase onto hydroxyapatite (HA) and hydroxyapatite-decorated ZrO2 (10%wt) (HA-ZrO2) 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-ZrO2 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-ZrO2 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-ZrO2 was shifted to pH 6.5 and 60 °C after immobilization. The immobilized α-amylase onto HA-ZrO2 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-ZrO2 is more sustainable and beneficial support for enzyme immobilization and it represents promising supports for different uses of α-amylase in the biomedical applications.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Almulaiky YQ,Khalil NM,El-Shishtawy RM,Altalhi T,Algamal Y,Aldhahri M,Al-Harbi SA,Allehyani ES,Bilal M,Mohammed MMdoi
10.1016/j.ijbiomac.2020.11.150subject
Has Abstractpub_date
2021-01-15 00:00:00pages
299-308eissn
0141-8130issn
1879-0003pii
S0141-8130(20)35074-1journal_volume
167pub_type
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