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2015 ; 5
(ä): 13184
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Doubling Power Output of Starch Biobattery Treated by the Most Thermostable
Isoamylase from an Archaeon Sulfolobus tokodaii
#MMPMID26289411
Cheng K
; Zhang F
; Sun F
; Chen H
; Percival Zhang YH
Sci Rep
2015[Aug]; 5
(ä): 13184
PMID26289411
show ga
Biobattery, 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?(o)C for 30?min. This enzyme was characterized and required
Mg(2+) as an activator. This enzyme was the most stable isoamylase reported with
a half lifetime of 200?min at 90?(o)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.