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Doubling Power Output of Starch Biobattery Treated by the Most Thermostable Isoamylase from an Archaeon Sulfolobus tokodaii.

Cheng K, Zhang F, Sun F, Chen H, Percival Zhang YH - Sci Rep (2015)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: College of Life Sciences, Henan Agricultural University, 95 Wenhua Road, Zhengzhou, 450002, China.

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus

Comparison of the conserved amino acid sequences in the active sites of isoamylases.Isoamylase sources (gene ID) are S. tokodaii (1458890), S. solfataricus (384432549), S. acidocaldaricus (568309602), E. coli F11 (190908135), Arthrobacter sp. (7648481), E. chrysanthemi (22074054), P. amylodermosa (151294), F. odoratum (5672639), B. lentus (493116169), and P. vulgaris (kidney bean) (139867062).
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f2: Comparison of the conserved amino acid sequences in the active sites of isoamylases.Isoamylase sources (gene ID) are S. tokodaii (1458890), S. solfataricus (384432549), S. acidocaldaricus (568309602), E. coli F11 (190908135), Arthrobacter sp. (7648481), E. chrysanthemi (22074054), P. amylodermosa (151294), F. odoratum (5672639), B. lentus (493116169), and P. vulgaris (kidney bean) (139867062).

Mentions: Figure 2 shows the three highly conserved amino acid sequences located in the catalytic domains among archaeal, bacterial and plant isoamylases. The three essential amino acid sites of this enzyme were Asp in region I, Glu in region II, and Asp in region III, in an agreement with Asp375, Glu435, and Asp510 of the P. amyloderamosa isoamylase, all of which play a catalytic role in activities of the α-amylase family21.


Doubling Power Output of Starch Biobattery Treated by the Most Thermostable Isoamylase from an Archaeon Sulfolobus tokodaii.

Cheng K, Zhang F, Sun F, Chen H, Percival Zhang YH - Sci Rep (2015)

Comparison of the conserved amino acid sequences in the active sites of isoamylases.Isoamylase sources (gene ID) are S. tokodaii (1458890), S. solfataricus (384432549), S. acidocaldaricus (568309602), E. coli F11 (190908135), Arthrobacter sp. (7648481), E. chrysanthemi (22074054), P. amylodermosa (151294), F. odoratum (5672639), B. lentus (493116169), and P. vulgaris (kidney bean) (139867062).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4542469&req=5

f2: Comparison of the conserved amino acid sequences in the active sites of isoamylases.Isoamylase sources (gene ID) are S. tokodaii (1458890), S. solfataricus (384432549), S. acidocaldaricus (568309602), E. coli F11 (190908135), Arthrobacter sp. (7648481), E. chrysanthemi (22074054), P. amylodermosa (151294), F. odoratum (5672639), B. lentus (493116169), and P. vulgaris (kidney bean) (139867062).
Mentions: Figure 2 shows the three highly conserved amino acid sequences located in the catalytic domains among archaeal, bacterial and plant isoamylases. The three essential amino acid sites of this enzyme were Asp in region I, Glu in region II, and Asp in region III, in an agreement with Asp375, Glu435, and Asp510 of the P. amyloderamosa isoamylase, all of which play a catalytic role in activities of the α-amylase family21.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: College of Life Sciences, Henan Agricultural University, 95 Wenhua Road, Zhengzhou, 450002, China.

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus