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P5420 Sigma

Pullulanase from Klebsiella pneumoniae

ammonium sulfate suspension, ≥5 units/mg protein (biuret)

Synonym: Amylopectin 6-gluconohydrolase, Limit dextrinase

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Description

Other Notes

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Preparation Note

Highly purified by a modification of ion exchange chromatography.

Unit Definition

One unit will liberate 1.0 μmole of maltotriose (measured as glucose) from pullulan per min at pH 5.0 at 25 °C.

Physical form

Suspension in 3.2 M (NH4)2SO4 solution, pH 6.2

Application

Pullulanase is a glycolytic enzyme from Klebsiella pneumoniae that is used to hydrolyze pullulan, an α-1,6-linked homopolymer of maltotriose. Product P5420 has been used to degrade carbohydrate from white beans Phaseolus vulgaris L. in healthy humans and to study pullulan biosynthesis.

The enzyme from Sigma has been used to estimate the pullulan content of the ethanol precipitates obtained from fermented agro-industrial wastes. It has also been used to the evaluate the branching of the maltodextrin fractions obtained from potato starch-derived maltodextrins (Paselli MD6) using ethanol precipitation methods.

Biochem/physiol Actions

Pullulanase hydrolyzes α-1,6 linkages of starch. Apart from pullulan, the enzyme also hydrolyzes α-1,6 linkages of amylopectin and glycogen. Maltose is the smallest sugar that it can release from an α-(1,6)-linkages.

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Biomedical Applications
Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3
Protocols & Articles

Articles

Ammonium Sulfate Suspensions - Technical Note

Note that for an ammonium sulfate suspension, most of the enzyme will be in solid form. It is likely that only negligible amounts of enzyme will be in the ammonium sulfate solution.
Keywords: Enzyme activity

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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