海藻酸钙水凝胶中包封的丙酮酸铁氧还蛋白氧化还原酶产生乙酰辅酶 A。
Acetyl-CoA production by encapsulated pyruvate ferredoxin oxidoreductase in alginate hydrogels.
机构信息
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.
出版信息
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。
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