Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement
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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Ital Publication
2023-10-01
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| Series: | Emerging Science Journal |
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| Online Access: | https://www.ijournalse.org/index.php/ESJ/article/view/1946 |
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| author | Yandri Yandri Hendri Ropingi Tati Suhartati Bambang Irawan Sutopo Hadi |
| author_facet | Yandri Yandri Hendri Ropingi Tati Suhartati Bambang Irawan Sutopo Hadi |
| author_sort | Yandri Yandri |
| collection | DOAJ |
| description | 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 50˚C, while the optimum temperature for α-amylase/bentonite/chitosan is 60˚C. The KM value of α-amylase/bentonite/chitosan was 1.69 ± 0.08 mg mL-1 substrate and the Vmax value was 52.32 ± 3.29 µmol mL-1 min-1, whereas for free α-amylase, the KM value of 2.56 ± 0.09 mg mL-1 substrate and the Vmax value of 3.78 ± 0.09 µmol mL-1 min-1 were obtained. The ΔGi value of free α-amylase is 102.68 ± 0.30 kJ mol-1 and the t½ is 21.23 ± 0.23 min, whereas the ΔGi value of α-amylase/bentonite/chitosan is 104.43 ± 0.00 kJ mol-1 and the t½ is 94.29 ± 0.91 min. The higher values of ΔGi and t½demonstrated 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
Full Text: PDF |
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| id | doaj.art-ae047233cf9d4db9b60fe78529859358 |
| institution | Directory Open Access Journal |
| issn | 2610-9182 |
| language | English |
| last_indexed | 2024-03-08T14:25:28Z |
| publishDate | 2023-10-01 |
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| series | Emerging Science Journal |
| spelling | doaj.art-ae047233cf9d4db9b60fe785298593582024-01-13T07:27:37ZengItal PublicationEmerging Science Journal2610-91822023-10-01751811182610.28991/ESJ-2023-07-05-023561Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability EnhancementYandri Yandri0Hendri Ropingi1Tati Suhartati2Bambang Irawan3Sutopo Hadi4Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,Department of Biology, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,Department of Chemistry, Faculty of Mathematics and Natural Sciences, University of Lampung, Bandar Lampung 35145,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 50˚C, while the optimum temperature for α-amylase/bentonite/chitosan is 60˚C. The KM value of α-amylase/bentonite/chitosan was 1.69 ± 0.08 mg mL-1 substrate and the Vmax value was 52.32 ± 3.29 µmol mL-1 min-1, whereas for free α-amylase, the KM value of 2.56 ± 0.09 mg mL-1 substrate and the Vmax value of 3.78 ± 0.09 µmol mL-1 min-1 were obtained. The ΔGi value of free α-amylase is 102.68 ± 0.30 kJ mol-1 and the t½ is 21.23 ± 0.23 min, whereas the ΔGi value of α-amylase/bentonite/chitosan is 104.43 ± 0.00 kJ mol-1 and the t½ is 94.29 ± 0.91 min. The higher values of ΔGi and t½demonstrated 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 Full Text: PDFhttps://www.ijournalse.org/index.php/ESJ/article/view/1946enzyme immobilizationα-amylasebentonite/chitosanaspergillus fumigatus. |
| spellingShingle | Yandri Yandri Hendri Ropingi Tati Suhartati Bambang Irawan Sutopo Hadi Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement Emerging Science Journal enzyme immobilization α-amylase bentonite/chitosan aspergillus fumigatus. |
| title | Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement |
| title_full | Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement |
| title_fullStr | Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement |
| title_full_unstemmed | Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement |
| title_short | Immobilization of Aspergillus fumigatus α-Amylase via Adsorption onto Bentonite/Chitosan for Stability Enhancement |
| title_sort | immobilization of aspergillus fumigatus α amylase via adsorption onto bentonite chitosan for stability enhancement |
| topic | enzyme immobilization α-amylase bentonite/chitosan aspergillus fumigatus. |
| url | https://www.ijournalse.org/index.php/ESJ/article/view/1946 |
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