The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from <em>Aspergillus niger</em> in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates
Lipase Amano A from <i>Aspergillus niger</i> (AA-ANL) is among the most commonly applied enzymes in biocatalysis processes, making it a significant scientific subject in the pharmaceutical and medical disciplines. In this study, we investigated the lipolytic activity of AA-ANL immobilize...
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MDPI AG
2022-08-01
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| Online Access: | https://www.mdpi.com/2073-4344/12/8/853 |
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| author | Tomasz Siódmiak Jacek Dulęba Natalia Kocot Dorota Wątróbska-Świetlikowska Michał Piotr Marszałł |
| author_facet | Tomasz Siódmiak Jacek Dulęba Natalia Kocot Dorota Wątróbska-Świetlikowska Michał Piotr Marszałł |
| author_sort | Tomasz Siódmiak |
| collection | DOAJ |
| description | Lipase Amano A from <i>Aspergillus niger</i> (AA-ANL) is among the most commonly applied enzymes in biocatalysis processes, making it a significant scientific subject in the pharmaceutical and medical disciplines. In this study, we investigated the lipolytic activity of AA-ANL immobilized onto polyacrylic support IB-150A in 23 oils of natural origin containing various amounts of polyunsaturated fatty acids (PUFAs) and monounsaturated fatty acids (MUFAs). The created systems were expressed as an ‘ESS catalytic triangle’. A distinct ‘jump’ (up to 2400%) of lipolytic activity of immobilized AA-ANL compared to free lipase and hyperactivation in mostly tested substrates was observed. There was a ‘cutoff limit’ in a quantitative mutual ratio of ω-PUFAs/MUFAs, for which there was an increase or decrease in the activity of the immobilized AA-ANL. In addition, we observed the beneficial effect of immobilization using three polyacrylic supports (IB-150A, IB-D152, and IB-EC1) characterized by different intramolecular interactions. The developed substrate systems demonstrated considerable hyperactivation of immobilized AA-ANL. Moreover, a ‘lipolytic jump’ in the full range of tested temperature and pH was also observed. The considerable activity of AA-ANL-IB-150A after four reuse cycles was demonstrated. On the other hand, we observed an essential decrease in stability of immobilized lipase after 168 h of storage in a climate chamber. The tested kinetic profile of immobilized AA-ANL confirmed the decreased affinity to the substrate relative to lipase in the free form. |
| first_indexed | 2024-03-09T04:36:49Z |
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| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-09T04:36:49Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Catalysts |
| spelling | doaj.art-5b654b84e4ce4996a13beae942c3dbf12023-12-03T13:26:06ZengMDPI AGCatalysts2073-43442022-08-0112885310.3390/catal12080853The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from <em>Aspergillus niger</em> in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin SubstratesTomasz Siódmiak0Jacek Dulęba1Natalia Kocot2Dorota Wątróbska-Świetlikowska3Michał Piotr Marszałł4Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Torun, 85-089 Bydgoszcz, PolandDepartment of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Torun, 85-089 Bydgoszcz, PolandDepartment of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Torun, 85-089 Bydgoszcz, PolandDepartment of Pharmaceutical Technology, Faculty of Pharmacy, Medical Biotechnology and Laboratory Medicine, Pomeranian Medical University in Szczecin, 71-251 Szczecin, PolandDepartment of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Torun, 85-089 Bydgoszcz, PolandLipase Amano A from <i>Aspergillus niger</i> (AA-ANL) is among the most commonly applied enzymes in biocatalysis processes, making it a significant scientific subject in the pharmaceutical and medical disciplines. In this study, we investigated the lipolytic activity of AA-ANL immobilized onto polyacrylic support IB-150A in 23 oils of natural origin containing various amounts of polyunsaturated fatty acids (PUFAs) and monounsaturated fatty acids (MUFAs). The created systems were expressed as an ‘ESS catalytic triangle’. A distinct ‘jump’ (up to 2400%) of lipolytic activity of immobilized AA-ANL compared to free lipase and hyperactivation in mostly tested substrates was observed. There was a ‘cutoff limit’ in a quantitative mutual ratio of ω-PUFAs/MUFAs, for which there was an increase or decrease in the activity of the immobilized AA-ANL. In addition, we observed the beneficial effect of immobilization using three polyacrylic supports (IB-150A, IB-D152, and IB-EC1) characterized by different intramolecular interactions. The developed substrate systems demonstrated considerable hyperactivation of immobilized AA-ANL. Moreover, a ‘lipolytic jump’ in the full range of tested temperature and pH was also observed. The considerable activity of AA-ANL-IB-150A after four reuse cycles was demonstrated. On the other hand, we observed an essential decrease in stability of immobilized lipase after 168 h of storage in a climate chamber. The tested kinetic profile of immobilized AA-ANL confirmed the decreased affinity to the substrate relative to lipase in the free form.https://www.mdpi.com/2073-4344/12/8/853Lipase Amano A from <i>Aspergillus niger</i>Immobead polyacrylic supportsvegetable oils of natural originfish oilPUFAsMUFAs |
| spellingShingle | Tomasz Siódmiak Jacek Dulęba Natalia Kocot Dorota Wątróbska-Świetlikowska Michał Piotr Marszałł The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from <em>Aspergillus niger</em> in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates Catalysts Lipase Amano A from <i>Aspergillus niger</i> Immobead polyacrylic supports vegetable oils of natural origin fish oil PUFAs MUFAs |
| title | The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from <em>Aspergillus niger</em> in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates |
| title_full | The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from <em>Aspergillus niger</em> in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates |
| title_fullStr | The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from <em>Aspergillus niger</em> in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates |
| title_full_unstemmed | The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from <em>Aspergillus niger</em> in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates |
| title_short | The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from <em>Aspergillus niger</em> in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates |
| title_sort | high lipolytic jump of immobilized amano a lipase from em aspergillus niger em in developed ess catalytic triangles containing natural origin substrates |
| topic | Lipase Amano A from <i>Aspergillus niger</i> Immobead polyacrylic supports vegetable oils of natural origin fish oil PUFAs MUFAs |
| url | https://www.mdpi.com/2073-4344/12/8/853 |
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