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dc.contributorVirginia Techen
dc.contributor.authorCheng, Kunen
dc.contributor.authorZhang, Feien
dc.contributor.authorSun, Fangfangen
dc.contributor.authorChen, Honggeen
dc.contributor.authorZhang, Y. H. Percivalen
dc.date.accessioned2017-03-13T17:13:41Zen
dc.date.available2017-03-13T17:13:41Zen
dc.date.issued2015-08-20en
dc.identifier.urihttp://hdl.handle.net/10919/76637en
dc.description.abstractBiobattery, a kind of enzymatic fuel cells, can convert organic compounds (e.g., glucose, starch) to electricity in a closed system without moving parts. Inspired by natural starch metabolism catalyzed by starch phosphorylase, isoamylase is essential to debranch alpha-1,6-glycosidic bonds of starch, yielding linear amylodextrin – the best fuel for sugar-powered biobattery. However, there is no thermostable isoamylase stable enough for simultaneous starch gelatinization and enzymatic hydrolysis, different from the case of thermostable alpha-amylase. A putative isoamylase gene was mined from megagenomic database. The open reading frame ST0928 from a hyperthermophilic archaeron Sulfolobus tokodaii was cloned and expressed in E. coli. The recombinant protein was easily purified by heat precipitation at 80 °C for 30 min. This enzyme was characterized and required Mg²⁺ as an activator. This enzyme was the most stable isoamylase reported with a half lifetime of 200 min at 90 °C in the presence of 0.5 mM MgCl₂, suitable for simultaneous starch gelatinization and isoamylase hydrolysis. The cuvett-based air-breathing biobattery powered by isoamylase-treated starch exhibited nearly doubled power outputs than that powered by the same concentration starch solution, suggesting more glucose 1-phosphate generated.en
dc.format.mimetypeapplication/pdfen
dc.language.isoen_USen
dc.publisherNatureen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleDoubling Power Output of Starch Biobattery Treated by the Most Thermostable Isoamylase from an Archaeon Sulfolobus tokodaiien
dc.typeArticle - Refereeden
dc.contributor.departmentBiological Systems Engineeringen
dc.title.serialScientific Reportsen
dc.identifier.doihttps://doi.org/10.1038/srep13184en
dc.identifier.volume5en
dc.type.dcmitypeTexten


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