A green approach to encapsulate proteins and enzymes within crystalline lanthanide-based Tb and Gd MOFs

Tocco D, Joshi M, Mastrangelo R, Fratini E, Salis A, Hartmann M (2024)


Publication Type: Journal article

Publication year: 2024

Journal

DOI: 10.1039/d4dt01667j

Abstract

In this work, bovine serum albumin (BSA) and Aspergillus sp. laccase (LC) were encapsulated in situ within two lanthanide-based MOFs (TbBTC and GdBTC) through a green one-pot synthesis (almost neutral aqueous solution, T = 25 °C, and atmospheric pressure) in about 1 h. Pristine MOFs and protein-encapsulated MOFs were characterized through wide angle X-ray scattering, scanning electron microscopy, thermogravimetric analysis, Fourier transform infrared and Raman spectroscopies. The location of immobilized BSA molecules, used as a model protein, was investigated through small angle X-ray scattering. BSA occurs both on the inner and on the outer surface of the MOFs. LC@TbBTC, and LC@GdBTC samples were also characterized in terms of specific activity, kinetic parameters, and storage stability both in water and acetate buffer. The specific activity of LC@TbBTC was almost twice that of LC@GdBTC (10.8 μmol min−1 mg−1vs. 6.6 μmol min−1 mg−1). Both biocatalysts showed similar storage stabilities retaining ∼60% of their initial activity after 7 days and ∼20% after 21 days. LC@TbBTC dispersed in acetate buffer exhibited a higher storage stability than LC@GdBTC. Additionally, terbium-based MOFs showed interesting luminescent properties. Together, these findings suggest that TbBTC and GdBTC are promising supports for the in situ immobilization of proteins and enzymes.

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APA:

Tocco, D., Joshi, M., Mastrangelo, R., Fratini, E., Salis, A., & Hartmann, M. (2024). A green approach to encapsulate proteins and enzymes within crystalline lanthanide-based Tb and Gd MOFs. Dalton Transactions. https://doi.org/10.1039/d4dt01667j

MLA:

Tocco, Davide, et al. "A green approach to encapsulate proteins and enzymes within crystalline lanthanide-based Tb and Gd MOFs." Dalton Transactions (2024).

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