Description

• General description: 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.[1] 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.[1]
• Application: α-Amylase from Bacillus sp. has been used: as a dispersal enzyme to test degradation of S. aureus biofilms[2], in the enzymatic hydrolysis of tapioca starch[3] in the enzymolysis of plant-based native and the amorphous granular starches[4]
• Biochem/physiol Actions: α-Amylase mediates the hydrolysis of starch, malto-oligosaccharides, and glycogen at the α-D-(1,4)-glucosidic linkages.[1] Bacillus sp. serve as an important cell factory for the heterogeneous production of α-amylase.[5] An extracellular secreted thermostable amylase from the Bacillus subtilis strain has also been reported.[6]
• Unit Definition: 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)
• Other Notes: Heat stability of bacterial α-amylases[7]; Action pattern on sweet potato starch, amylose and amylopectin[8]; Action on native wheat starch.[9]