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- W3115115507 endingPage "124611" @default.
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- W3115115507 abstract "α-L-Rhamnosidase (Rha) is a biotechnologically important enzyme that degrades biomass containing natural rhamnoside. Herein, the recombinant Rha was successfully immobilized on magnetic metal-organic frameworks (MOFs), and used to hydrolyze rutin. Magnetic MOFs were constructed by binding Cu2+ and PABA to the surface of Fe3O4 nanoparticles coated with a polydopamine film through coordinate covalent bonds, and the enzyme was attached to the MOFs using the cross-linking agents EDC/NHS. The immobilized enzyme [email protected] reached an activity of 25.09 U/g with a lower apparent Km value compared with the free enzyme. The conversion rate of 20 g/L rutin was 91.42%, corresponding to an isoquercitrin productivity of 12.78 g/L/h. [email protected] also exhibited significantly improved reusability; the conversion rate was still 73.55% after 30 cycles at 60 °C. These results indicated that the magnetic MOF-immobilized enzyme was a feasible biocatalyst for the conversion of flavonoids with low aqueous solubility." @default.
- W3115115507 created "2021-01-05" @default.
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- W3115115507 date "2021-03-01" @default.
- W3115115507 modified "2023-10-18" @default.
- W3115115507 title "Immobilization of alpha-L-rhamnosidase on a magnetic metal-organic framework to effectively improve its reusability in the hydrolysis of rutin" @default.
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- W3115115507 doi "https://doi.org/10.1016/j.biortech.2020.124611" @default.
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