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E2412

Sigma-Aldrich

Pullulanase microbial

Synonyme(s) :

Pullulanase microbial, Promozyme® D2

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About This Item

Numéro CAS:
9075-68-7
Numéro de classification (Commission des enzymes):
3.2.1.41 (BRENDA, IUBMB)
Numéro MDL:
MFCD00081941
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in Bacillus subtilis

Forme

aqueous solution

Activité spécifique

≥1000 NPUN/g

Température de stockage

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.

Actions biochimiques/physiologiques

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

Autres remarques

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

Informations légales

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

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

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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
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
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
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
Guodong Liu et al.
Carbohydrate polymers, 98(1), 995-1001 (2013-08-31)
This study aims to investigate the physicochemical and extended-release properties of amorphous debranched starch (ADBS) that is a linear short chain amylose derived from pullulanase enzymatic modification. The results show the completely amorphous ADBS was soluble in cold water, which
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