Comparison of chitin and Amberlite IRA-938 for alpha-galactosidase immobilization.
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.
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Department of Biochemistry, Faculty of Science, Ege University, Bornova-Izmir, Turkey. tatar@sci.ege.edu.tr
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D000837:Anion Exchange Resins / Q000737:chemistry / Q000592:standards*; D002219:Carbamates / Q000737:chemistry* / Q000592:standards; D002686:Chitin / Q000737:chemistry* / Q000592:standards; D029773:Citrullus / Q000201:enzymology; D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000592:standards; D007093:Imidazoles / Q000737:chemistry* / Q000592:standards; D008722:Methods; D000519:alpha-Galactosidase / Q000737:chemistry*; D005680:gamma-Aminobutyric Acid
D000837:Anion Exchange Resins; D002219:Carbamates; D003432:Cross-Linking Reagents; D004800:Enzymes, Immobilized; C477860:IRA-938; D007093:Imidazoles; D002686:Chitin; D005680:gamma-Aminobutyric Acid; C006900:N,N-carbonyldiimidazole; D000519:alpha-Galactosidase