Pullulanase M1 (Klebsiella planticola)

High purity Pullulanase M1 (Klebsiella planticola) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

EC 3.2.1.41
CAZy Family: GH13
CAS: 9075-68-7 

pullulanase; pullulan 6-alpha-glucanohydrolase

Highly purified. From Klebsiella planticola. Electrophoretically homogeneous.
In 3.2 M ammonium sulphate.
Supplied at ~ 700 U/mL. 

Specific activity:
~ 30 U/mg (40oC, pH 5.0 on pullulan). 

Stability: > 4 years at 4oC.

Recommended pullulanase for research on starch structure.

Product Code
Content/size
Stock
Price
Qty
E-PULKP
700 Units
$199.00

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DESCRIPTION

Pullulanase M1 (Klebsiella planticola)

EC 3.2.1.41
CAZy Family: GH13
CAS: 9075-68-7 

Synonyms:
pullulanase; pullulan 6-alpha-glucanohydrolase

Form:
In 3.2 M ammonium sulphate.

Stability: 
> 4 years at 4oC.

Specific activity:
~ 30 U/mg (40oC, pH 5.0 on pullulan).

Unit definition:
One Unit of pullulanase M2 activity is defined as the amount of enzyme required to release one µmole of glucose reducing-sugar-equivalents per minute from pullulan (5 mg/mL) in sodium acetate buffer (100 mM), pH 5.0 at 40oC.

Specificity:
Hydrolysis of (1,6)-α-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the α- and β-limit dextrins of amylopectin and glycogen.

Applications:
Applications in the cereals, food and feeds industries particularly in starch saccharification and production of high glucose or maltose syrups.

Deficiency of maize starch-branching enzyme i results in altered starch fine structure, decreased digestibility and reduced coleoptile growth during germination.

Xia, H., Yandeau-Nelson, M., Thompson, D. B. & Guiltinan, M. J. (2011). BMC Plant Biology, 11(1), 95-107.

Rapid determination of enzyme purity by a microdialysis-based assay.

Richardson, S., Nilsson, G. S., Torto, N., Gorton, L. & Laurell, T. (1999). Analytical Communications, 36(5), 189-193.

Enzyme-aided investigation of the substituent distribution in cationic potato amylopectin starch.

Richardson, S., Nilsson, G., Cohen, A., Momcilovic, D., Brinkmalm, G. & Gorton, L. (2003). Analytical Chemistry, 75(23), 6499-6508.

Residual amylopectin structures of amylase-treated wheat starch slurries reflect amylase mode of action.

Leman, P., Goesaert, H. & Delcour, J. A. (2009). Food Hydrocolloids, 23(1), 153-164.

Differences in structures of starch hydrolysates using saliva from different individuals.

Nantanga, K. K. M., Chan, E., Suleman, S., Bertoft, E. & Seetharaman, K. (2013). Starch‐Stärke, 65(7‐8), 709-713.

Structures of human salivary amylase hydrolysates from starch processed at two water concentrations.

Nantanga, K. K. M., Bertoft, E. & Seetharaman, K. (2013). Starch‐Stärke, 65(7‐8), 637-644.

Debranching of β-dextrins to explore branching patterns of amylopectins from three maize genotypes.

Xia, H. & Thompson, D. B. (2006). Cereal Chemistry, 83(6), 668-676.

Effects of Chemical and Enzymatic Modifications on Starch–Oleic Acid Complex Formation.

Arijaje, E. O. & Wang, Y. J. (2015). Journal of Agricultural and Food Chemistry, 63(16), 4202-4210.

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