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Immobilization and characterization of bovine liver catalase on eggshell
Author(s) -
Özlem Alptekin,
S. Seyhan Tükel,
Deniz Yıldırım
Publication year - 2008
Publication title -
journal of the serbian chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.227
H-Index - 45
eISSN - 1820-7421
pISSN - 0352-5139
DOI - 10.2298/jsc0806609a
Subject(s) - catalase , eggshell , chemistry , chromatography , enzyme , reusability , nuclear chemistry , biochemistry , biology , ecology , software , computer science , programming language
Bovine liver catalase immobilized on eggshell particles was charac- terized 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 opti- mum 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 1.4×10 6 and 2.8×10 3 dm 3 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.

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