BIOAFFINITY ADSORPTION BEHAVIOR OF SEVERAL ENZYMES ONTO BETA-CYCLODEXTRIN-CHITOSAN

Citation
S. Harsa et S. Furusaki, BIOAFFINITY ADSORPTION BEHAVIOR OF SEVERAL ENZYMES ONTO BETA-CYCLODEXTRIN-CHITOSAN, Separation science and technology, 30(13), 1995, pp. 2695-2706
Citations number
6
Categorie Soggetti
Engineering, Chemical","Chemistry Analytical
ISSN journal
01496395
Volume
30
Issue
13
Year of publication
1995
Pages
2695 - 2706
Database
ISI
SICI code
0149-6395(1995)30:13<2695:BABOSE>2.0.ZU;2-0
Abstract
In this study, specific and nonspecific adsorption and desorption of a lpha-amylase, lactase, and amyloglucosidase (AMG) enzymes onto the bet a-cyclodextrin (CD)-chitosan system were investigated. alpha-Amylase a nd lactase enzymes were adsorbed onto the chitosan-only and chitosan-s pacer gels, but very little adsorption was observed in the case of the chitosan gels with CD. Furthermore, AMG enzyme showed a high degree o f interaction with CD immobilized on chitosan. Therefore, the interact ion between the AMG and CD molecules can be explained by the fact that there is true biospecific adsorption. Desorption experiments also con firm this theory because the elution of AMG was much more difficult th an the elution of lactase and alpha-amylase from the CD matrix.