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beta amylase/arachis hypogaea
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An antioxidant rich novel β-amylase from peanuts (Arachis hypogaea): Its purification, biochemical characterization and potential applications.
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β-Amylase from un-germinated seeds of peanut (Arachis hypogaea) was purified to apparent electrophoretic homogeneity with final purification fold of 205 and specific activity of 361μmol/min/mg protein. The enzyme was purified employing simple purification techniques for biochemical characterization.
Enzymatic hydrolysis of native granular starches by a new β-amylase from peanut (Arachis hypogaea).
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The present work describes efficient hydrolysis of native starch by a novel β-amylase from peanut (Arachis hypogaea). The Dextrose Equivalent value, which is a measure of starch hydrolysis, for potato and corn starch increased significantly by 40% and 10%, respectively, releasing maltose. Scanning
Purification to homogeneity and characterization of a 1,3-beta-glucan (callose) synthase from germinating Arachis hypogaea cotyledons.
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A 1,3-beta-D-glucan (callose) synthase (CS) from a plasma membrane fraction of germinating peanut (Arachis hypogaea L.) cotyledons has been purified to apparent homogeneity as evidenced by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), amino-terminal analysis, and the Western
Covalent immobilization of peanut β-amylase for producing industrial nano-biocatalysts: A comparative study of kinetics, stability and reusability of the immobilized enzyme.
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Stability of enzymes is an important parameter for their industrial applicability. Here, we report successful immobilization of β-amylase (bamyl) from peanut (Arachis hypogaea) onto Graphene oxide-carbon nanotube composite (GO-CNT), Graphene oxide nanosheets (GO) and Iron oxide nanoparticles
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