α-Amylase from Bacillus sp.

α-Amylase (α-1,4-glucan-4-glucanohydrolase) belongs to the glycosyl hydrolase family 13. The two aspartic residues and one glutamic acid residue are the prime catalytic residues of α-amylase. All amylases have three domain regions, namely, domain A with a central (β/α)8 barrel, domain B, and β-structure with a Greek key motif encompassing domain C.

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch hydrolysis research. For more information see the article in biofiles.

α-Amylase from Bacillus sp. has been used:

• as a dispersal enzyme to test degradation of S. aureus biofilms,
• in the enzymatic hydrolysis of tapioca starch
• in the enzymolysis of plant-based native and the amorphous granular starches

Heat stability of bacterial α-amylases; Action pattern on sweet potato starch, amylose and amylopectin; Action on native wheat starch.

α-Amylase mediates the hydrolysis of starch, malto-oligosaccharides, and glycogen at the α-D-(1,4)-glucosidic linkages. Bacillus sp. serve as an important cell factory for the heterogeneous production of α-amylase. An extracellular secreted thermostable amylase from the Bacillus subtilis strain has also been reported.

One unit is the amount of enzyme which liberates 1 μmole of maltose per minute at pH 6.9 and 25°C (using Cat. No. 85642 as substrate)