Molecular recognition of an acyl–enzyme intermediate on the lipase B from <i>Candida antarctica</i>
This investigation provides evidence of the acyl enzyme species involved in the interaction of <i>R/S</i>ketoprofen with the lipase B from <i>Candida antarctica</i>. The interaction between the profen and the enzyme was studied by <i>in situ</i> time-resolved ATR-...
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| Autores principales: | , , , , |
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| Formato: | Articulo |
| Lenguaje: | Español |
| Publicado: |
2017
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| Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/105708 https://pubs.rsc.org/en/content/articlelanding/2017/CY/C7CY00245A |
| Aporte de: |
| Sumario: | This investigation provides evidence of the acyl enzyme species involved in the interaction of <i>R/S</i>ketoprofen with the lipase B from <i>Candida antarctica</i>. The interaction between the profen and the enzyme was studied by <i>in situ</i> time-resolved ATR-FTIR under both static and transient conditions. Particularly, modulation excitation spectroscopy (MES) with phase sensitive detection (PSD) allowed us to univocally distinguish the signals belonging to the interaction between ketoprofen and the enzyme from the strong background signals. These experimental tools coupled with theoretical DFT analysis allowed us to propose various species derived from the interaction of ketoprofen with serine through H bonding (without reaction) and the acyl enzyme species (ester bond formation) which are the intermediates in the biocatalytic assisted esterification and hydrolysis using lipases. |
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