Abstract
An amylase from Bacillus polymyxa was purified by ammonium sulfate and organic solvent precipitations. This amylase produces β-maltose as the predominant product when reacting with amylose, amylopectin, and glycogen. It catalyzes the degradation of maltooctaose to given maltose, maltotriose, and maltotetraose as the predominant early stage products. It also catalyzes the degradation of the Schardinger dextrins to given maltose and maltotriose as products. Bacillus polymyxa amylase resembles the α-amylases found in animals and bacteria by being able to bypass the α-1→6 linkages of amylopectin and glycogen and by not requiring a nonreducing end for action. It resembles the β-amylases of higher plants by producing β-maltose as the predominant product from α-1→4 glucosans. It does not resemble any of the previously described α or β-amylases in that it catalyzes the degradation of the Schardinger dextrins.
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