International Institute for Carbon-Neutral Energy Research (WPI-I(2)CNER), Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan; Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan.
International Institute for Carbon-Neutral Energy Research (WPI-I(2)CNER), Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan; Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan; Centre for Small Molecule Energy, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan.
Bioresour Technol. 2017 Mar;227:279-285. doi: 10.1016/j.biortech.2016.12.051. Epub 2016 Dec 18.
Pyruvate ferredoxin oxidoreductase from Citrobacter sp. S-77 (PFOR) was purified in order to develop a method for acetyl-CoA production. Although the purified PFOR showed high O-sensitivity, the activity could be remarkably stabilized in anaerobic conditions. PFOR was effectively immobilized on ceramic hydroxyapatite (PFOR-HA) with an efficiency of more than 96%, however, after encapsulation of PFOR-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-HA in alginate hydrogels was remarkable, retaining over 68% initial activity even after ten repeated cycles. The results suggested that the PFOR-HA hydrogels have a high potential for biotechnological application.
为了开发乙酰辅酶 A 的生产方法，对柠檬酸杆菌 S-77（PFOR）的丙酮酸铁氧还蛋白氧化还原酶进行了纯化。尽管纯化的 PFOR 表现出对 O2 的高度敏感性，但在厌氧条件下，其活性可以得到显著稳定。PFOR 可以有效地固定在陶瓷羟磷灰石（PFOR-HA）上，效率超过 96%，然而，当 PFOR-HA 被包埋在藻酸盐中时，与游离酶相比，催化乙酰辅酶 A 生成的速率大大降低至 36%。然而，PFOR-HA 在藻酸盐水凝胶中的操作稳定性非常显著，即使经过十次重复循环，仍保留超过 68%的初始活性。结果表明，PFOR-HA 水凝胶在生物技术应用方面具有很高的潜力。
