Stability and activity of hydrogenases of Methanobacterium thermoautotrophicum and Alcaligenes eutrophus in reversed micellar systems.
In water-in-oil microemulsion the membrane-associated F420-hydrogenase of Methanobacterium thermoautotrophicum (strain Marburg) and the membrane-bound hydrogenase of Alcaligenes eutrophus H 16 (MBH) showed prolonged activity at elevated temperatures (measured as hydrogen production) as compared to aqueous buffer solution. The temperature optimum of the reactions was about 15 degrees C higher than in aqueous buffer solution. Activity of the almost completely inactivated F420-hydrogenase could be partially recovered by transfer into microemulsion.
Hoppert
M
M
Institut für Mikrobiologie, Georg-August-Universität Göttingen, FRG.
Braks
I
I
Mayer
F
F
D000421:Alcaligenes / Q000201:enzymology*; D000473:Alkanes; D004655:Emulsions; D004793:Enzyme Reactivators; D004795:Enzyme Stability; D006601:Hexoses; D017014:Methanobacterium / Q000201:enzymology*; D008823:Micelles; D008956:Models, Chemical; D010088:Oxidoreductases / Q000378:metabolism*; D011136:Polysorbates
D000473:Alkanes; D004655:Emulsions; D004793:Enzyme Reactivators; D006601:Hexoses; D008823:Micelles; D011136:Polysorbates; C018665:sorbitan monooleate; D010088:Oxidoreductases; C033895:coenzyme F420 hydrogenase; C007932:n-hexadecane