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

• Published in: International journal of biological macromolecules Vol. 96; pp. 111 - 117
• Main Authors: Brassesco, Ma. Emilia, Woitovich Valetti, Nadia, Picó, Guillermo
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2017
• Subjects: Adsorption; Alginate; Alginates - chemistry; Animals; Egg White - chemistry; Epichlorohydrin - chemistry; Galactans - chemistry; Glucuronic Acid - chemistry; Guar gum; Hexuronic Acids - chemistry; Kinetics; Lysozyme; Mannans - chemistry; Muramidase - chemistry; Plant Gums - chemistry; Polyelectrolytes; GG; Adsorption; Guar gum; Polyelectrolytes; Alginate; Alg; LZ; Lysozyme; Epi
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2016.12.029

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 2.4mg 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 0.3M 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.