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Journal of Materials Science

, Volume 52, Issue 23, pp 13378–13389 | Cite as

Hydrochar as protein support: preservation of biomolecule properties with non-covalent immobilization

  • Manuela Oliveira Castro
  • Mayara Queiroz de Santiago
  • Kyria Santiago Nascimento
  • Benildo Sousa Cavada
  • Emilio de Castro Miguel
  • Amauri Jardim de Paula
  • Odair Pastor FerreiraEmail author
Biomaterials
  • 257 Downloads

Abstract

In this work, the ConBr lectin was non-covalently immobilized onto hydrochar (HC). This carbonaceous material was produced by the hydrothermal carbonization of glucose and then put to interact with the lectin, aiming to immobilize the biomolecule via electrostatic interactions. Samples obtained after the interaction were characterized by CHNS elemental analysis, scanning electron microscopy and Fourier transform infrared spectroscopy (FTIR). FTIR results from the conjugated sample identified the presence of NH2 + and NH3 + groups of the protein and COO groups of the HC, indicating the occurrence of electrostatic interaction between the biomolecule and the support. Furthermore, the immobilization experiment was also performed using ConBr lectin marked with fluorescein isothiocyanate to assess the immobilization on the hydrochar using fluorescence emission analysis. Hemagglutination tests revealed that even after the conjugation with the HC, the agglutinating property of lectin toward erythrocytes (red blood cells) was preserved. Finally, our results indicate that non-covalent interactions represent an efficient mechanism for protein immobilization on the HC while maintaining the protein structure and its biological activity.

Notes

Acknowledgements

The authors acknowledge Francisco Holanda Soares Júnior for the SEM images and Antonio Gomes de Souza Filho for the precious discussions. Also, the authors are grateful to Central Analítida-UFC/CT-INFRA/MCTI-SISNANO/Pró-Equipamentos CAPES for providing the electron scanning microscopes and confocal fluorescence microscope and CETENE for the TEM measurements. This work was supported by CNPq (Grant 478743/2013-0), FUNCAP (PRONEX PR2-0101-00006.01.00/15) and CAPES (for the scholarship awarded to M. O. Castro).

Supplementary material

10853_2017_1441_MOESM1_ESM.pdf (2.2 mb)
Supplementary material 1 (PDF 2253 kb)

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Copyright information

© Springer Science+Business Media, LLC 2017

Authors and Affiliations

  1. 1.Laboratório de Materiais Funcionais Avançados (LaMFA), Departamento de FísicaUniversidade Federal do CearáFortalezaBrazil
  2. 2.Laboratório de Moléculas Biologicamente Ativas (BioMol - Lab), Departamento de Bioquímica e Biologia MolecularUniversidade Federal do CearáFortalezaBrazil
  3. 3.Central Analítica, Departamento de FísicaUniversidade Federal do CearáFortalezaBrazil
  4. 4.Solid-Biological Interface Group (SolBIN), Departamento de FísicaUniversidade Federal do CearáFortalezaBrazil

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