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E2412

Sigma-Aldrich

Pullulanase microbial

Synonym(s):

Pullulanase microbial, Promozyme® D2

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About This Item

CAS Number:
9075-68-7
Enzyme Commission number:
3.2.1.41 (BRENDA, IUBMB)
MDL number:
MFCD00081941
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in Bacillus subtilis

form

aqueous solution

specific activity

≥1000 NPUN/g

storage temp.

2-8°C

Application

Pullulanase is a glucanase that degrades pullulan. It is commonly used for starch-debranching as well as to study polysaccharide utilization.

Biochem/physiol Actions

Type I pullulanases specifically hydrolyse α-1,6 linkages, while type II pullulanases are also able to hydrolyse α-1,4 linkages.

Other Notes

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

Legal Information

A product of Novozymes Corp.
Novozym is a registered trademark of Novozymes A/S
Promozyme is a trademark of Novozymes Corp.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Nasima Chorfa et al.
Polymers, 14(10) (2022-05-29)
In this work, a valorization of the starch stemming from downgraded potatoes was approached through the preparation of starch nanoparticles using different physical methods, namely liquid and supercritical carbon dioxide, high energy ball milling (HEBM), and ultrasonication on the one
Christopher C Ibenegbu et al.
Microbial cell factories, 21(1), 251-251 (2022-11-30)
The starch in waste bread (WB) from industrial sandwich production was directly converted to ethanol by an amylolytic, ethanologenic thermophile (Parageobacillus thermoglucosidasius strain TM333) under 5 different simultaneous saccharification and fermentation (SSF) regimes. Crude α-amylase from TM333 was used alone
K A Smith et al.
Journal of bacteriology, 171(4), 2116-2123 (1989-04-01)
We have cloned a pullulanase gene from Bacteroides thetaiotaomicron. The pullulanase expressed from this clone in Escherichia coli was cell associated and soluble and had a molecular mass of 72 kilodaltons by gel filtration. Maxicell analysis of proteins coded by
Johanne Mørch Jensen et al.
Protein expression and purification, 79(2), 217-222 (2011-05-05)
The limit dextrinase inhibitor (LDI) from barley seeds acts specifically on limit dextrinase (LD), an endogenous starch debranching enzyme. LDI is a 14 kDa hydrophobic protein containing four disulfide bonds and one unpaired thiol group previously found to be either
Malene Bech Vester-Christensen et al.
Journal of molecular biology, 403(5), 739-750 (2010-09-25)
Barley limit dextrinase [Hordeum vulgare limit dextrinase (HvLD)] catalyzes the hydrolysis of α-1,6 glucosidic linkages in limit dextrins. This activity plays a role in starch degradation during germination and presumably in starch biosynthesis during grain filling. The crystal structures of
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