α-Amylase (Aspergillus oryzae

High purity α-Amylase (Aspergillus oryzae) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

EC 3.2.1.1
CAZy Family: GH13
CAS: 9000-90-2

alpha-amylase; 4-alpha-D-glucan glucanohydrolase

From Aspergillus oryzae.
In 3.2 M ammonium sulphate.
Supplied at ~ 1,000 CU/mL.  

Specific activity:
~ 120 U/mg (40oC, pH 5.4 on Ceralpha Reagent).

Stability: > 4 years at 4oC. As used in Megazyme Starch Damage method.

Product Code
Content/size
Stock
Price
Qty
E-ANAAM
20,000 Units
$182.00

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

DESCRIPTION

α-Amylase (Aspergillus oryzae)

EC 3.2.1.1
CAZy Family: GH13
CAS: 9000-90-2

Synonyms:
alpha-amylase; 4-alpha-D-glucan glucanohydrolase

Form:
In 3.2 M ammonium sulphate.

Stability: 
> 4 years at 4oC.  As used in Megazyme Starch Damage method.

Specific activity:
~ 120 U/mg (40oC, pH 5.4 on Ceralpha Reagent).

Unit definition:.
One Unit of α-amylase is the amount of enzyme required to release one μmole of p-nitrophenol from blocked p-nitrophenyl-maltoheptaoside per minute (in the presence of excess α-glucosidase), pH 5.4 at 40oC, and is termed a Ceralpha Unit.

Specificity:
endo-hydrolysis of α-1,4-D-glucosidic linkages in starch.

Applications:
For use in Megazyme Starch Damage method.

New developments in the measurement of α-amylase, endo-protease, β-glucanase and β-xylanase.

McCleary, B. V. & Monaghan, D. (2000). “Proceedings of the Second European Symposium on Enzymes in Grain Processing”, (M. Tenkanen, Ed.), VTT Information Service, pp. 31-38.

Measurement of cereal α-Amylase: A new assay procedure.

McCleary, B. V. & Sheehan, H. (1987). Journal of Cereal Science, 6(3), 237-251.

A new procedure for the measurement of fungal and bacterial α-amylase.

Sheehan, H. & McCleary, B. V. (1988). Biotechnology Techniques, 2(4), 289-292.

An improved enzymic method for the measurement of starch damage in wheat flour.

Gibson, T. S., Al Qalla, H. & McCleary, B. V. (1992). Journal of Cereal Science, 15(1), 15-27.

Measurement of α-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the ceralpha assay: Collaborative study.

McCleary, B. V., McNally, M., Monaghan, D. & Mugford, D. C. (2002). Journal of AOAC International, 85(5), 1096-1102.

Increasing the energy density of vegetative tissues by diverting carbon from starch to oil biosynthesis in transgenic Arabidopsis.

Sanjaya, Durrett, T. P., Weise, S. E. & Benning, C. (2011). Plant Biotechnology Journal, 9(8), 874-883.

Characterisation of the substituent distribution in hydroxypropylated potato amylopectin starch.

Richardson, S., Nilsson, G. S., Bergquist, K. E., Gorton, L. & Mischnick, P. (2000). Carbohydrate Research, 328(3), 365-373.

Engineering starch accumulation by manipulation of phosphate metabolism of starch.

Weise, S. E., Aung, K., Jarou, Z. J., Mehrshahi, P., Li, Z., Hardy, A. C., Carr, D. J. & Sharkey, T. D. (2012). Plant Biotechnology Journal, 10(5), 545-554.

Spatial division of phosphoenolpyruvate carboxylase and nitrate reductase activity and its regulation by cytokinins in CAM-induced leaves of Guzmania monostachia (Bromeliaceae).

Pereira, P. N., Purgatto, E. & Mercier, H. (2013). Journal of Plant Physiology, 170(12), 1067-1074.

Nitrogen metabolism in leaves of a tank epiphytic bromeliad: Characterization of a spatial and functional division.

Takahashi, C. A. & Mercier, H. (2011). Journal of Plant Physiology, 168(11), 1208-1216.

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.

Hydrolysis of amylopectin by amylolytic enzymes: level of inner chain attack as an important analytical differentiation criterion.

Goesaert, H., Bijttebier, A. & Delcour, J. A. (2010). Carbohydrate Research, 345(3), 397-401.

Hydrolysis of Maltoheptaose in Flow through Silicon Wafer Microreactors Containing Immobilised α‐Amylase and Glycoamylase.

Melander, C., Tüting, W., Bengtsson, M., Laurell, T., Mischnick, P. & Gorton, L. (2006). Starch‐Stärke, 58(5), 231-242.

Proteins from multiple metabolic pathways associate with starch biosynthetic enzymes in high molecular weight complexes: a model for regulation of carbon allocation in maize amyloplasts.

Hennen-Bierwagen, T. A., Lin, Q., Grimaud, F., Planchot, V., Keeling, P. L., James, M. G. & Myers, A. M. (2009). Plant Physiology, 149(3), 1541-1559.

Characterization of the Paenibacillus beijingensis DSM 24997 GtfD and its glucan polymer products representing a new glycoside hydrolase 70 subfamily of 4,6-α-glucanotransferase enzymes.

Gangoiti, J., Lamothe, L., van Leeuwen, S. S., Vafiadi, C. & Dijkhuizen, L. (2017). PloS One, 12(4), e0172622.