β-Amylase from sweet potato

β-Amylases belongs to the class of amylolytic enzymes.

Substrate Specificity

Hydrolysis of (1→4)-α-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains

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β -Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. β -Amylase, from Sigma, has been used in various plant studies, such as carbon starvation studies in Populus tremuloides. β-amylase from sweet potato has been used to examine the utility of the enzyme in inhibiting and removing Staphylococcus aureus biofilms. The enzyme has also been used to prepare β-limit dextrin from waxy maize starch.

β-Amylase from sweet potato has been used:

• in the hydrolysis of starch and starch-pectin combinations
• for comparing amylases from different sources in Staphylococcus aureus SH1000 biofilm inhibition and reduction assay
• for selenium speciation in samples

β-Amylases plays a major role in examining enzymatic promiscuity among glycosidases.

β-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose. β-amylase from sweet potato is a tetramer of identical subunits, which are arranged to exhibit 222 molecular symmetry.

Crystalline suspension in 2.3 M (NH₄)₂SO₄

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 4.8 at 20 °C.

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer