Comparison of Chitin and Amberlite IRA‐938 for α‐Galactosidase Immobilization
Makaleler > Tam Makale · 2003
Yazarlar: Seçil ÖNAL, AZMİ TELEFONCU
Artificial Cells, Blood Substitutes, and Biotechnology, SCI Expanded İndekslerine Giren Dergi, Uluslararası, Wos, 2003, cilt 31, ss 19-33
Özet
Watermelon alpha-galactosidase (EC 3.2.1.22) was immobilized on a natural (chitin) and a synthetic anion-exchange (Amberlite IRA-938) support by covalent coupling methods. The procedure entails the activation of supports with 1,1'-carbonyldiimidazole (CDI), followed by immobilization of the enzyme on to these supports without and with a spacer arm; gamma-aminobutyric acid (GABA). Optimization of activation was performed by changing the CDI concentrations and coupling efficiencies. The comparison of two immobilization techniques for both chitin and Amberlite IRA-938 was made by comparing different enzyme concentrations against enzyme activity yield. Furthermore, the storage stability of the immobilized enzymes was also investigated and chitin immobilized alpha-galactosidase was found to be better. Although the activity yield of immobilized enzymes were the same for both supports, the short storage stability of immobilized enzyme on Amberlite IRA-938 is currently a drawback to its applications.