Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization
This work presents a framework for evaluating hybrid nanoflowers using <i>Burkholderia cepacia</i> lipase. It was expanded on previous findings by testing lipase hybrid nanoflowers (hNF-lipase) formation over a wide range of pH values (5–9) and buffer concentrations (10–100 mM). The free...
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MDPI AG
2024-01-01
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| author | Danivia Endi S. Souza Lucas M. F. Santos João P. A. Freitas Lays C. de Almeida Jefferson C. B. Santos Ranyere Lucena de Souza Matheus M. Pereira Álvaro S. Lima Cleide M. F. Soares |
| author_facet | Danivia Endi S. Souza Lucas M. F. Santos João P. A. Freitas Lays C. de Almeida Jefferson C. B. Santos Ranyere Lucena de Souza Matheus M. Pereira Álvaro S. Lima Cleide M. F. Soares |
| author_sort | Danivia Endi S. Souza |
| collection | DOAJ |
| description | This work presents a framework for evaluating hybrid nanoflowers using <i>Burkholderia cepacia</i> lipase. It was expanded on previous findings by testing lipase hybrid nanoflowers (hNF-lipase) formation over a wide range of pH values (5–9) and buffer concentrations (10–100 mM). The free enzyme activity was compared with that of hNF-lipase. The analysis, performed by molecular docking, described the effect of lipase interaction with copper ions. The morphological characterization of hNF-lipase was performed using scanning electron microscopy. Fourier Transform Infrared Spectroscopy performed the physical–chemical characterization. The results show that all hNF-lipase activity presented values higher than that of the free enzyme. Activity is higher at pH 7.4 and has the highest buffer concentration of 100 mM. Molecular docking analysis has been used to understand the effect of enzyme protonation on hNF-lipase formation and identify the main the main binding sites of the enzyme with copper ions. The hNF-lipase nanostructures show the shape of flowers in their micrographs from pH 6 to 8. The spectra of the nanoflowers present peaks typical of the amide regions I and II, current in lipase, and areas with P–O vibrations, confirming the presence of the phosphate group. Therefore, hNF-lipase is an efficient biocatalyst with increased catalytic activity, good nanostructure formation, and improved stability. |
| first_indexed | 2024-03-08T03:52:02Z |
| format | Article |
| id | doaj.art-ad9185c794194dc3bc2ba03db0bb4b52 |
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| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-08T03:52:02Z |
| publishDate | 2024-01-01 |
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| series | Molecules |
| spelling | doaj.art-ad9185c794194dc3bc2ba03db0bb4b522024-02-09T15:18:53ZengMDPI AGMolecules1420-30492024-01-0129362810.3390/molecules29030628Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase ImmobilizationDanivia Endi S. Souza0Lucas M. F. Santos1João P. A. Freitas2Lays C. de Almeida3Jefferson C. B. Santos4Ranyere Lucena de Souza5Matheus M. Pereira6Álvaro S. Lima7Cleide M. F. Soares8Postgraduate Program Process Engineering, Tiradentes University (UNIT), Campus Farolandia, Aracaju 49032-490, Sergipe, BrazilPostgraduate Program Process Engineering, Tiradentes University (UNIT), Campus Farolandia, Aracaju 49032-490, Sergipe, BrazilPostgraduate Program Process Engineering, Tiradentes University (UNIT), Campus Farolandia, Aracaju 49032-490, Sergipe, BrazilPostgraduate Program Process Engineering, Tiradentes University (UNIT), Campus Farolandia, Aracaju 49032-490, Sergipe, BrazilPostgraduate Program Process Engineering, Tiradentes University (UNIT), Campus Farolandia, Aracaju 49032-490, Sergipe, BrazilPostgraduate Program Process Engineering, Tiradentes University (UNIT), Campus Farolandia, Aracaju 49032-490, Sergipe, BrazilDepartment of Chemical Engineering, University of Coimbra, CIEPQPF, 3030-790 Coimbra, PortugalPostgraduate Program Chemical Engineering, Federal University of Bahia (UFBA), Campus Federação, Salvador 40210-630, Bahia, BrazilPostgraduate Program Process Engineering, Tiradentes University (UNIT), Campus Farolandia, Aracaju 49032-490, Sergipe, BrazilThis work presents a framework for evaluating hybrid nanoflowers using <i>Burkholderia cepacia</i> lipase. It was expanded on previous findings by testing lipase hybrid nanoflowers (hNF-lipase) formation over a wide range of pH values (5–9) and buffer concentrations (10–100 mM). The free enzyme activity was compared with that of hNF-lipase. The analysis, performed by molecular docking, described the effect of lipase interaction with copper ions. The morphological characterization of hNF-lipase was performed using scanning electron microscopy. Fourier Transform Infrared Spectroscopy performed the physical–chemical characterization. The results show that all hNF-lipase activity presented values higher than that of the free enzyme. Activity is higher at pH 7.4 and has the highest buffer concentration of 100 mM. Molecular docking analysis has been used to understand the effect of enzyme protonation on hNF-lipase formation and identify the main the main binding sites of the enzyme with copper ions. The hNF-lipase nanostructures show the shape of flowers in their micrographs from pH 6 to 8. The spectra of the nanoflowers present peaks typical of the amide regions I and II, current in lipase, and areas with P–O vibrations, confirming the presence of the phosphate group. Therefore, hNF-lipase is an efficient biocatalyst with increased catalytic activity, good nanostructure formation, and improved stability.https://www.mdpi.com/1420-3049/29/3/628lipase hybrid nanoflowerselectrostatic interactionsenzyme protonation |
| spellingShingle | Danivia Endi S. Souza Lucas M. F. Santos João P. A. Freitas Lays C. de Almeida Jefferson C. B. Santos Ranyere Lucena de Souza Matheus M. Pereira Álvaro S. Lima Cleide M. F. Soares Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization Molecules lipase hybrid nanoflowers electrostatic interactions enzyme protonation |
| title | Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization |
| title_full | Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization |
| title_fullStr | Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization |
| title_full_unstemmed | Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization |
| title_short | Experimental and Computational Analysis of Synthesis Conditions of Hybrid Nanoflowers for Lipase Immobilization |
| title_sort | experimental and computational analysis of synthesis conditions of hybrid nanoflowers for lipase immobilization |
| topic | lipase hybrid nanoflowers electrostatic interactions enzyme protonation |
| url | https://www.mdpi.com/1420-3049/29/3/628 |
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