The purification of a novel amylase from Bacillus subtilis and its inhibition by wheat proteins.
A new alpha-amylase (EC 3.2.1.1) from Bacillus subtilis was purified by affinity chromatography. The molecular weight of the purified enzyme, estimated from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, was 93000, which is very different from the molecular weights of two well-characterized amylases from B. subtilis. Electrofocusing showed an isoelectric point of 5. Amylase shows a broad maximum of activity between pH 6 and 7; maximal inhibition of enzyme by wheat-protein alpha-amylase inhibitors is displayed at pH 7.
D000681:Amylases / Q000302:isolation & purification*; D001412:Bacillus subtilis / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010940:Plant Proteins / Q000494:pharmacology*; D014908:Triticum; D000516:alpha-Amylases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*
D010940:Plant Proteins; D000681:Amylases; D000516:alpha-Amylases