title: Stability and reactivity of liposome-encapsulated formate dehydrogenase and cofactor system in carbon dioxide gas-liquid flow.
abstract: Formate dehydrogenase from Candida boidinii (CbFDH) is potentially applicable in reduction of CO(2) through oxidation of cofactor NADH into NAD(+). For this, the CbFDH activity needs to be maintained under practical reaction conditions, such as CO(2) gas-liquid flow. In this work, CbFDH and cofactor were encapsulated in liposomes and the liposomal enzymes were characterized in an external loop airlift bubble column. The airlift was operated at 45 degrees C with N(2) or CO(2) as gas phase at the superficial gas velocity U(G) of 2.0 or 3.0 cm/s. The activities of liposomal CbFDH/cofactor systems were highly stable in the airlift regardless of the type of gas phase because liposome membranes prevented interactions of the encapsulated enzyme and cofactor molecules with the gas-liquid interface of bubbles. On the other hand, free CbFDH was deactivated in the airlift especially at high U(G) with CO(2) bubbles. The liposomal CbFDH/NADH could catalyze reduction of CO(2) in the airlift giving the fractional oxidation of the liposomal NADH of 23% at the reaction time of 360 min. The cofactor was kept inside liposomes during the reaction operation with less than 10% of leakage. All of the results obtained demonstrate that the liposomal CbFDH/NADH functions as a stable catalyst for reduction of CO(2) in the airlift.
authors: Department of Applied Molecular Bioscience, Yamaguchi University, 2-16-1 Tokiwadai, Ube, Japan. yosimoto@yamaguchi-u.ac.jp
authors: Makoto
authors: M
authors: Yoshimoto
authors: Takayuki
authors: T
authors: Yamashita
authors: Takuya
authors: T
authors: Yamashiro
mesh_terms: D002175:Candida / Q000201:enzymology; D002245:Carbon Dioxide / Q000737:chemistry*; D004795:Enzyme Stability; D005560:Formate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism*; D008081:Liposomes / Q000737:chemistry*
chemical_list: D008081:Liposomes; D002245:Carbon Dioxide; D005560:Formate Dehydrogenases