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'-NH, 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 degrees C is the most suitable condition. Alpha-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%.
Wang
Yun
Y
College of Bioscience and Biotechnology, Yangzhou University, China. wangy1974@263.net
Guo
Mingliang
M
Jiang
Yongming
Y
D000447:Aldehydes / Q000737:chemistry*; D002686:Chitin / Q000031:analogs & derivatives* / Q000737:chemistry*; D048271:Chitosan; D002853:Chromatography, Liquid / Q000295:instrumentation*; D009994:Osmolar Concentration; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D000516:alpha-Amylases / Q000302:isolation & purification
D000447:Aldehydes; D002686:Chitin; D048271:Chitosan; C046012:pentanal; D000516:alpha-Amylases