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Journal ArticleDOI

d-Amino Acid Oxidase Immobilized on Pt Nanoparticle-Loaded Porous SiO2 Nanospheres Coated with a Zirconium-Based Coordination Polymer for Catalytic Deamination of d-Alanine

26 Nov 2021-Vol. 4, Iss: 11, pp 12373-12381
About: The article was published on 2021-11-26. It has received 1 citations till now. The article focuses on the topics: Coordination polymer & Deamination.
Citations
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Journal Article
TL;DR: In this article, the rotational mobility of lipase and bovine serum albumin was investigated in five types of mesoporous silica particles with different pore and particle sizes exploiting the intrinsic UV-vis absorption and fluorescence anisotropy of the tryptophan residues.
Abstract: Enzyme immobilization in porous silica particles is used to improve enzyme function in biocatalytic applications. Here, we study the effective protein concentration and rotational mobility of lipase and bovine serum albumin in the pores, when confined in five types of mesoporous silica particles with different pore and particle sizes, exploiting the intrinsic UV–vis absorption and fluorescence anisotropy of the tryptophan residues. For all investigated combinations of proteins and particles, the steady-state anisotropy is higher than for the same protein in free solution, indicating a slower protein rotation inside the pores. The retardation is stronger in more narrow pores, but the proteins can still move, and there is no dependence on the particle size. The average number of proteins per particle, Nₚᵣₒₜ, varies with the particle diameter, D, as Nₚᵣₒₜ ∼ D².⁹⁵±⁰.⁰² for both proteins, which is close to the scaling D³.⁰±⁰.¹ for the available pore volume. This observation indicates that both proteins are distributed evenly throughout the particles and rules out that the proteins are only externally bound to the particle surface. Secondly, the concentration of the protein in the pores depends on the pore and protein size but not on the particle size and corresponds to volume fractions in the range of 20–60%.

29 citations

References
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TL;DR: This review focuses on recent advances in methodology for enzyme immobilization on carbon nanotubes for fabrication of biosensors and biofuel cells and for preparation of biocatalysts.

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TL;DR: Modification of the enzymes immobilized on supports that did not offer the possibility of react with glutaraldehyde showed the same stability that the non modified preparations demonstrating that the mere chemical modification did not have effect on the enzyme stability.

279 citations