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Cobiss

Journal of the Serbian Chemical Society 2008 Volume 73, Issue 6, Pages: 609-618
https://doi.org/10.2298/JSC0806609A
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Immobilization and characterization of bovine liver catalase on eggshell

Alptekin Özlem (University of Çukurova, Faculty of Sciences and Letters, Department of Chemistry, Adana, Turkey)
Tükel Seyhan S. (University of Çukurova, Faculty of Sciences and Letters, Department of Chemistry, Adana, Turkey)
Yildirim Deniz (University of Çukurova, Faculty of Sciences and Letters, Department of Chemistry, Adana, Turkey)

Bovine liver catalase immobilized on eggshell particles was characterized and the reusability of the immobilized catalase was investigated in a batch type reactor. For immobilized catalase onto ground eggshell (ICATG), the optimum initial amount of catalase was 85 mg g-1 of eggshells, the optimum pH was 6.0 (75 mM citrate buffer) and the temperature was 30°C. The Vmax and Km values of ICATG were determined as 29.1±1.2 U/mg of protein and 41.9±2.7 mM, respectively. The reusability of ICATG was tested and the remaining activity of ICATG was found to be 73% of the initial activity after 80 cycles of batch operation. The amount of catalase bound onto the carrier was estimated by using the results of induced coupled plasma measurements. The catalytic efficiencies (kcat/Km) of free catalase and ICATG were found to be 1.4x106 and 2.8x103 dm3 s-1 mol-1, respectively. Catalase immobilization onto eggshell is economic and has good reusability. Hence, it can be concluded that eggshell is an efficient carrier for immobilizing catalase.

Keywords: catalase, eggshell, immobilization, glutaraldehyde, induced coupled plasma