Application of Immobilized Cholest-4-en-3-one Δ<sup>1</sup>-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of Steroids
Cholest-4-en-3-one Δ<sup>1</sup>-dehydrogenase (AcmB) from <i>Sterolibacterium denitrificans</i> was successfully immobilized on 3-aminopropyltrimethoysilane functionalized mesoporous cellular foam (MCF) and Santa Barbara Amorphous (SBA-15) silica supports using adsorption or...
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MDPI AG
2020-12-01
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| author | Mateusz Tataruch Patrycja Wójcik Agnieszka M. Wojtkiewicz Katarzyna Zaczyk Katarzyna Szymańska Maciej Szaleniec |
| author_facet | Mateusz Tataruch Patrycja Wójcik Agnieszka M. Wojtkiewicz Katarzyna Zaczyk Katarzyna Szymańska Maciej Szaleniec |
| author_sort | Mateusz Tataruch |
| collection | DOAJ |
| description | Cholest-4-en-3-one Δ<sup>1</sup>-dehydrogenase (AcmB) from <i>Sterolibacterium denitrificans</i> was successfully immobilized on 3-aminopropyltrimethoysilane functionalized mesoporous cellular foam (MCF) and Santa Barbara Amorphous (SBA-15) silica supports using adsorption or covalently with glutaraldehyde or divinyl sulfone linkers. The best catalyst, AcmB on MCF linked covalently with glutaraldehyde, retained the specific activity of the homogenous enzyme while exhibiting a substantial increase of the operational stability. The immobilized enzyme was used continuously in the fed-batch reactor for 27 days, catalyzing 1,2-dehydrogenation of androst-4-en-3-one to androst-1,4-dien-3-one with a final yield of 29.9 mM (8.56 g/L) and 99% conversion. The possibility of reuse of the immobilized catalyst was also demonstrated and resulted in a doubling of the product amount compared to that in the reference homogenous reactor. Finally, it was shown that molecular oxygen from the air can efficiently be used as an electron acceptor either reoxidizing directly the enzyme or the reduced 2,4-dichlorophenolindophenol (DCPIPH<sub>2</sub>). |
| first_indexed | 2024-03-10T14:05:32Z |
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| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T14:05:32Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-089b9dfcee7c4021ab3a4931f253b48d2023-11-21T00:41:16ZengMDPI AGCatalysts2073-43442020-12-011012146010.3390/catal10121460Application of Immobilized Cholest-4-en-3-one Δ<sup>1</sup>-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of SteroidsMateusz Tataruch0Patrycja Wójcik1Agnieszka M. Wojtkiewicz2Katarzyna Zaczyk3Katarzyna Szymańska4Maciej Szaleniec5Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Kraków, PolandJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Kraków, PolandJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Kraków, PolandJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Kraków, PolandDepartment of Chemical Engineering and Process Design, Silesian University of Technology, Ks. M. Strzody 7, 44-100 Gliwice, PolandJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Kraków, PolandCholest-4-en-3-one Δ<sup>1</sup>-dehydrogenase (AcmB) from <i>Sterolibacterium denitrificans</i> was successfully immobilized on 3-aminopropyltrimethoysilane functionalized mesoporous cellular foam (MCF) and Santa Barbara Amorphous (SBA-15) silica supports using adsorption or covalently with glutaraldehyde or divinyl sulfone linkers. The best catalyst, AcmB on MCF linked covalently with glutaraldehyde, retained the specific activity of the homogenous enzyme while exhibiting a substantial increase of the operational stability. The immobilized enzyme was used continuously in the fed-batch reactor for 27 days, catalyzing 1,2-dehydrogenation of androst-4-en-3-one to androst-1,4-dien-3-one with a final yield of 29.9 mM (8.56 g/L) and 99% conversion. The possibility of reuse of the immobilized catalyst was also demonstrated and resulted in a doubling of the product amount compared to that in the reference homogenous reactor. Finally, it was shown that molecular oxygen from the air can efficiently be used as an electron acceptor either reoxidizing directly the enzyme or the reduced 2,4-dichlorophenolindophenol (DCPIPH<sub>2</sub>).https://www.mdpi.com/2073-4344/10/12/14603-ketosteroid Δ<sup>1</sup>-dehydrogenaseKSTDKSDHAcmB1,2-dehydrogenationcholest-4-en-3-one Δ<sup>1</sup>-dehydrogenase |
| spellingShingle | Mateusz Tataruch Patrycja Wójcik Agnieszka M. Wojtkiewicz Katarzyna Zaczyk Katarzyna Szymańska Maciej Szaleniec Application of Immobilized Cholest-4-en-3-one Δ<sup>1</sup>-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of Steroids Catalysts 3-ketosteroid Δ<sup>1</sup>-dehydrogenase KSTD KSDH AcmB 1,2-dehydrogenation cholest-4-en-3-one Δ<sup>1</sup>-dehydrogenase |
| title | Application of Immobilized Cholest-4-en-3-one Δ<sup>1</sup>-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of Steroids |
| title_full | Application of Immobilized Cholest-4-en-3-one Δ<sup>1</sup>-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of Steroids |
| title_fullStr | Application of Immobilized Cholest-4-en-3-one Δ<sup>1</sup>-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of Steroids |
| title_full_unstemmed | Application of Immobilized Cholest-4-en-3-one Δ<sup>1</sup>-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of Steroids |
| title_short | Application of Immobilized Cholest-4-en-3-one Δ<sup>1</sup>-Dehydrogenase from Sterolibacterium Denitrificans for Dehydrogenation of Steroids |
| title_sort | application of immobilized cholest 4 en 3 one δ sup 1 sup dehydrogenase from sterolibacterium denitrificans for dehydrogenation of steroids |
| topic | 3-ketosteroid Δ<sup>1</sup>-dehydrogenase KSTD KSDH AcmB 1,2-dehydrogenation cholest-4-en-3-one Δ<sup>1</sup>-dehydrogenase |
| url | https://www.mdpi.com/2073-4344/10/12/1460 |
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