Mesoporous silica are versatile materials with wide-ranging potential. Notably, they excel as enzyme supports. This work examines the influence of three distinct siliceous mesoporous materials used as supports for the enzyme human lactate dehydrogenase (hLDH-A). Drugs with inhibition effects have recently shown favorable effects on diminishing the proliferation of cancerous cells. The ultimate goal of this research is to produce a stable and effective biocatalyst suitable for being employed in a microreactor for the screening of hLDH-A inhibitors. The synthesized mesoporous silica exhibited distinctive structural features, including a quasi-mesocellular network, bent-channels structure, and a dendritic geometry with radial symmetry, as evidenced by FESEM and HR-TEM. These materials were functionalized with amino and aldehyde groups to covalently immobilize hLDH-A. Characterization of both pristine and functionalized materials involved a comprehensive examination of their physico-chemical properties. The CO dosing revealed Brønsted acidity characteristic of mesoporous silica, while FT-IR spectroscopy and N2 physisorption at 77 K confirmed their successful functionalization. Enzyme immobilization on the functionalized supports, performed with stabilizing agents such as PEG (0.05 mg/ml) or trehalose (300 mM), produced promising results. The immobilization yield consistently exceeded 80 %, with retained activity reaching values as high as 15 %. The immobilization of the enzyme on mesoporous silica increased the stability of hLDH-A against alkaline and organic solutions. These findings hold significance for those exploring siliceous porous supports for enzyme immobilization, paving the way for the development of stable and active biocatalysts.
Synthesis and characterization of mesoporous silicas with dendritic and spongy-like structures: potential supports for human lactate dehydrogenase-based microreactors aimed at anticancer inhibitor screening / Cocuzza, Clarissa; Vincenzi, Chiara; Ottone, Carminna; Illanes, Andrés; Fino, Debora; Cauda, Valentina; Piumetti, Marco. - In: MICROPOROUS AND MESOPOROUS MATERIALS. - ISSN 1387-1811. - ELETTRONICO. - 376:(2024), p. 113182. [10.1016/j.micromeso.2024.113182]
Synthesis and characterization of mesoporous silicas with dendritic and spongy-like structures: potential supports for human lactate dehydrogenase-based microreactors aimed at anticancer inhibitor screening
Cocuzza, Clarissa;Ottone, Carminna;Fino, Debora;Cauda, Valentina;Piumetti, Marco
2024
Abstract
Mesoporous silica are versatile materials with wide-ranging potential. Notably, they excel as enzyme supports. This work examines the influence of three distinct siliceous mesoporous materials used as supports for the enzyme human lactate dehydrogenase (hLDH-A). Drugs with inhibition effects have recently shown favorable effects on diminishing the proliferation of cancerous cells. The ultimate goal of this research is to produce a stable and effective biocatalyst suitable for being employed in a microreactor for the screening of hLDH-A inhibitors. The synthesized mesoporous silica exhibited distinctive structural features, including a quasi-mesocellular network, bent-channels structure, and a dendritic geometry with radial symmetry, as evidenced by FESEM and HR-TEM. These materials were functionalized with amino and aldehyde groups to covalently immobilize hLDH-A. Characterization of both pristine and functionalized materials involved a comprehensive examination of their physico-chemical properties. The CO dosing revealed Brønsted acidity characteristic of mesoporous silica, while FT-IR spectroscopy and N2 physisorption at 77 K confirmed their successful functionalization. Enzyme immobilization on the functionalized supports, performed with stabilizing agents such as PEG (0.05 mg/ml) or trehalose (300 mM), produced promising results. The immobilization yield consistently exceeded 80 %, with retained activity reaching values as high as 15 %. The immobilization of the enzyme on mesoporous silica increased the stability of hLDH-A against alkaline and organic solutions. These findings hold significance for those exploring siliceous porous supports for enzyme immobilization, paving the way for the development of stable and active biocatalysts.File | Dimensione | Formato | |
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https://hdl.handle.net/11583/2988964