Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement

Yandri Yandri; Hendri Ropingi; Tati Suhartati; Bambang Irawan; Sutopo Hadi

doi:10.28991/ESJ-2023-07-05-023

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Yandri Yandri
yandri.as@fmipa.unila.ac.id
Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,, Indonesia
Hendri Ropingi Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,, Indonesia
Tati Suhartati Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,, Indonesia
Bambang Irawan Department of Biology, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,, Indonesia
Sutopo Hadi Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,, Indonesia

Vol. 7 No. 5 (2023): October

Research Articles

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Stability enhancement attempted in this study demonstrated that significant improvement in the stability of the α-amylase isolated from Aspergillus fumigatus was achieved by immobilizing the enzyme on a bentonite/chitosan hybrid matrix using the adsorption method. Centrifugation was used to isolate the α-amylase, which was then refined using (NH₄)₂SO₄ salt precipitation and dialysis. The purity of the α-amylase improved 19.40 times when compared to that of the crude extract. The optimal temperature for free α-amylase is 50ËšC, while the optimum temperature for α-amylase/bentonite/chitosan is 60ËšC. The K_M value of α-amylase/bentonite/chitosan was 1.69 ± 0.08 mg mL^-1 substrate and the V_max value was 52.32 ± 3.29 µmol mL^-1 min^-1, whereas for free α-amylase, the K_M value of 2.56 ± 0.09 mg mL^-1 substrate and the V_max value of 3.78 ± 0.09 µmol mL^-1 min^-1 were obtained. The Î”G_i value of free α-amylase is 102.68 ± 0.30 kJ mol^-1 and the t_½ is 21.23 ± 0.23 min, whereas the Î”G_i value of α-amylase/bentonite/chitosan is 104.43 ± 0.00 kJ mol^-1 and the t_½ is 94.29 ± 0.91 min. The higher values of Î”G_i and t_½demonstrated that α-amylase/bentonite/chitosan has better stability than that of free α-amylase. Another important finding is that α-amylase /bentonite/chitosan was able to retain their activity as high as 47.61 ± 0.53% after six recycles, indicating that the enzyme has the potential to be used in industry.

Doi: 10.28991/ESJ-2023-07-05-023

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Yandri, Y., Ropingi, H., Suhartati, T., Irawan, B., & Hadi, S. (2023). Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement. Emerging Science Journal, 7(5), 1811–1826. https://doi.org/10.28991/ESJ-2023-07-05-023

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Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement

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Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement

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