초록
Pyruvate ferredoxin oxidoreductase from Citrobacter sp. S-77 (PFOR<SUB>S77</SUB>) was purified in order to develop a method for acetyl-CoA production. Although the purified PFOR<SUB>S77</SUB> showed high O<SUB>2</SUB>-sensitivity, the activity could be remarkably stabilized in anaerobic conditions. PFOR<SUB>S77</SUB> was effectively immobilized on ceramic hydroxyapatite (PFOR<SUB>S77</SUB>-HA) with an efficiency of more than 96%, however, after encapsulation of PFOR<SUB>S77</SUB>-HA in alginate, the rate of catalytic acetyl-CoA production was highly reduced to 36% when compared to that of the free enzyme. However, the operational stability of the PFOR<SUB>S77</SUB>-HA in alginate hydrogels was remarkable, retaining over 68% initial activity even after ten repeated cycles. The results suggested that the PFOR<SUB>S77</SUB>-HA hydrogels have a high potential for biotechnological application.