Molecular mechanism of lysozyme adsorption onto chemically modified alginate guar gum matrix

Maria Emilia Brassesco, Nadia Woitovich Valetti, Guillermo Picó*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)


The equilibrium isotherms and adsorption kinetics of lysozyme (LZ) on epichlorohydrin (Epi) cross-linked alginate-guar gum (Alg-GG) matrix were studied. Adsorption kinetics followed a pseudo-first-order model while the equilibrium isotherm could be represented by the Freundlich equation. The maximal amount of LZ adsorbed onto this matrix was around 2.4 mg per g of hydrated matrix at pH 7.00. The adsorption mechanism was associated to a simple diffusion process with a weak columbic interaction between LZ and the matrix. The presence of NaCl 0.3 M induced a total displacement of the LZ from the matrix. Under this condition, the percentage of desorbed protein was 95%. Successive cycles of adsorption-washing-elution were performed and the results showed the reversibility of the process and the usefulness of the method for enzyme purification and separation. A last successful step was carried out for the purification of LZ from egg white as natural source. The model proved to be useful applied as a platform design in the isolation and purification of proteins.
Original languageEnglish
Pages (from-to)111-117
Number of pages7
JournalInternational Journal of Biological Macromolecules
Publication statusPublished - 1 Mar 2017
Externally publishedYes


  • Adsorption
  • Alginate
  • Guar gum
  • Lysozyme
  • Polyelectrolytes


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