Evaluation of n-valeraldehyde modified chitosan as a matrix for hydrophobic interaction chromatography

The n-valeraldehyde modified Chitosan (pentyl-Chitosan CL) was prepared by Schiff-base formation and hydrogenation. By studying the IR spectra of Chitosan and pentyl-Chitosan CL, it is suggested that a pentyl group is linked to 2′-NH2 by a C–N bond. The influence of temperature and ionic strength on the adsorption of protein on pentyl-Chitosan CL were studied, and it was found that the behavior of adsorption met with the theory of hydrophobic interaction. The storage stability of these packing materials was also investigated, the results show storage in 20% ethanol at 4 °C is the most suitable condition. α-Amylase was purified successfully by hydrophobic interaction chromatography, using pentyl-Chitosan CL as hydrophobic matrix. The purification factor is about 2.5 and the recovery is over 82%.