Acetyl-CoA production by encapsulated pyruvate ferredoxin oxidoreductase in alginate hydrogels

- PFOR was anaerobically purified from Citrobacter sp. S-77.
- Ceramic hydroxyapatite acted as a stable matrix of PFORS77 in alginate hydrogels.
- Efficient acetyl-CoA production by the immobilized PFOR was achieved.
- The PFORS77-HA hydrogels had remarkable reusability under anaerobic conditions.

Pyruvate ferredoxin oxidoreductase from Citrobacter sp. S-77 (PFORS77) was purified in order to develop a method for acetyl-CoA production. Although the purified PFORS77 showed high O2-sensitivity, the activity could be remarkably stabilized in anaerobic conditions. PFORS77 was effectively immobilized on ceramic hydroxyapatite (PFORS77-HA) with an efficiency of more than 96%, however, after encapsulation of PFORS77-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 PFORS77-HA in alginate hydrogels was remarkable, retaining over 68% initial activity even after ten repeated cycles. The results suggested that the PFORS77-HA hydrogels have a high potential for biotechnological application.

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