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ATP regeneration by thermostable ATP synthase
Author(s) -
Nam Ki Y.,
Struck Douglas K.,
Holtzapple Mark T.
Publication year - 1996
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19960805)51:3<305::aid-bit6>3.0.co;2-h
Subject(s) - atp synthase , liposome , electrodialysis , chemistry , reagent , base (topology) , thermophile , membrane , biochemistry , yield (engineering) , chromatography , enzyme , organic chemistry , materials science , mathematical analysis , mathematics , metallurgy
We investigated the possibility of using thermostable ATP synthase (TF 0 F 1 ) for a new ATP regeneration method. TF 0 F 1 was purified from a thermophilic bacterium, PS3, and reconstituted into liposomes. ATP synthesis experiments showed that TF 0 F 1 liposomes could synthesize ATP in micromole concentrations by acid–base change. The acid–base change was repeated six times over an 11‐day period with no detectable loss of activity at the reaction temperature (45°C). Given these encouraging results, we conceptualized and modeled a system to synthesize ATP using ATP synthase with energy supplied by acid–base change. In this system, liposomes containing ATP synthase are immobilized on small glass spheres that facilitate separation of buffers from the liposomes after the acid–base change. Compared to an alternate system that uses membranes to separate the buffers from the liposomes, the glass spheres reduce inefficient mixing of acidic and basic buffers during the acid–base change. To increase the ATP synthesis yield, this system uses electrodialysis to regenerate a potassium gradient after the acid–base change. It also employs water‐splitting electrodialysis to regenerate KOH and HCl required to adjust the pH of acidic and basic buffers. All reagents are recycled, so electrical energy is the only required input. © 1996 John Wiley & Sons, Inc.