Isoamylase HP (Glycogen 6-glucanohydrolase) 

High purity Isoamylase HP (Glycogen 6-glucanohydrolase) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

CAZy Family: GH13
CAS: 9067-73-6 

isoamylase; glycogen 6-alpha-D-glucanohydrolase

Highly purified. From Pseudomonas sp. Electrophoretically homogeneous.
In 3.2 M ammonium sulphate.
Supplied at ~ 500 U/mL.

Specific activity: 
~ 240 U/mg (40oC, pH 4.0 on oyster glycogen) (equivalent to 16 MU Sigma Units/mg).

Stability: > 4 years at 4oC. 

Product Code
200 Units

In association with DHL Express Megazyme offers expedited same day shipping on all orders received before 12 noon GMT, DHL offers express shipping to over 220 countries worldwide serving 35 countries next day and 65 within 2 days. For further details visit our delivery page. Should delivery error or damage require you to return a product please contact our Customer Service team to obtain shipping instructions and authorisation. For full terms and conditions see T&Cs.

We support the following payment methods:

  • Visa
  • MasterCard
  • American Express
  • Cheque
  • Wire Transfer / EFT /ACH

For further details visit our payment page


Isoamylase HP (Glycogen 6-glucanohydrolase)

CAZy Family: GH13
CAS: 9067-73-6 

isoamylase; glycogen 6-alpha-D-glucanohydrolase

In 3.2 M ammonium sulphate.

> 4 years at 4oC.

Specific activity:
~ 240 U/mg (40oC, pH 4.0 on oyster glycogen) (equivalent to 16 MU Sigma Units/mg).

Unit definition:
One unit of isoamylase activity is the amount of enzyme required to release one μmole of D-glucose reducing sugar equivalent in the presence of oyster glycogen per min at pH 4.0 and 40oC.

Hydrolysis of (1,6)-α-D-glucosidic branch linkages in glycogen, amylopectin and their β-limit dextrins.

Applications in carbohydrate research and in the food and feeds, and cereals industry.

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.

Effect of a gibberellin-biosynthesis inhibitor treatment on the physicochemical properties of sorghum starch.

Li, E., Hasjim, J., Dhital, S., Godwin, I. D. & Gilbert, R. G. (2011). Journal of Cereal Science, 53(3), 328-334.

Characterization of starch granules in rice culms for application of rice straw as a feedstock for saccharification.

Matsuki, J., Park, J. Y., Shiroma, R., Arai-Sanoh, Y., Ida, M., Kondo, M., Motobayashi, K. & Tokuyasu, K. (2010). Bioscience, Biotechnology, and Biochemistry, 74(8), 1645-1651.

Physico-chemical properties of potato starches.

Alvani, K., Qi, X., Tester, R. F. & Snape, C. E. (2011). Food Chemistry, 125(3), 958-965.

Determination of polydextrose as dietary fiber in foods.

Craig, S. A. S., Holden, J. F. & Khaled, M. Y. (2000). Journal of AOAC International, 83(4), 1006-1012.

Amylolysis of wheat starches. II. Degradation patterns of native starch granules with varying functional properties.

Blazek, J. & Copeland, L. (2010). Journal of Cereal Science, 52(2), 295-302.

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.

Determination of polydextrose in foods by ion chromatography: collaborative study.

Craig, S. A. S., Holden, J. F. & Khaled, M. Y. (2001). Journal of AOAC International, 84(2), 472-478.

Structure and function of starch and resistant starch from corn with different doses of mutant amylose-extender and floury-1 alleles.

Yao, N., Paez, A. V. & White, P. J. (2009). Journal of Agricultural and Food Chemistry, 57(5), 2040-2048.

Molecular structure and granule morphology of native and heat‐moisture‐treated pinhão starch.

Pinto, V. Z., Moomand, K., Vanier, N. L., Colussi, R., Villanova, F. A., Zavareze, E. R., Lim, L. T. & Dias, A. R. G. (2015). International Journal of Food Science & Technology, 50(2), 282-289.

An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment.

Vester, J. K., Glaring, M. A. & Stougaard, P. (2015). Applied Microbiology and Biotechnology, 99(2), 717-727.

Below you will find a link to our dedicated frequently asked questions section. Within this section you will find common questions and answers on a range of topics about the product.