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Highly Efficient Regioselective Decanoylation of Hyperoside Using Nanobiocatalyst of Fe(3)O(4)@PDA-Thermomyces lanuginosus Lipase: Insights of Kinetics and Stability Evaluation
The immobilization of Thermomyces lanuginosus lipase on polydopamine-functionalized Fe(3)O(4) magnetic nanoparticles (Fe(3)O(4)@PDA-TLL) as a nanobiocatalyst was successfully performed for the first time, and the Fe(3)O(4)@PDA-TLL was used for regioselective acylation of natural hyperoside with viny...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7270339/ https://www.ncbi.nlm.nih.gov/pubmed/32548099 http://dx.doi.org/10.3389/fbioe.2020.00485 |
Sumario: | The immobilization of Thermomyces lanuginosus lipase on polydopamine-functionalized Fe(3)O(4) magnetic nanoparticles (Fe(3)O(4)@PDA-TLL) as a nanobiocatalyst was successfully performed for the first time, and the Fe(3)O(4)@PDA-TLL was used for regioselective acylation of natural hyperoside with vinyl decanoate. The effects of several crucial factors, such as the reaction solvent, substrate molar ratio, temperature, and immobilized enzyme dosage, were investigated. Under optimum conditions, the reaction rate, 6″-regioselectivity, and maximum substrate conversion were as high as 12.6 mM/h, 100%, and 100%, respectively. An operational stability study demonstrated that the immobilized enzyme could maintain 90.1% of its initial maximum conversion even after reusing it five times. In addition, further investigations on the kinetic parameters, like V(max), K(m), V(max)/K(m), and E(a), also revealed that the biocompatible Fe(3)O(4)@PDA could act as an alternative carrier for the immobilization of different enzymes. |
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