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We characterized ramie leaf β-amylase, and determined its thermostability and kinetic parameters. The enzyme was purified 53-fold using ammonium sulfate fractionation (40–60% saturation), anion exchange chromatography on DEAE-cellulose and gel permeation chromatography on Superdex-200. The purified enzyme was identified as β-amylase with molecular mass of 42kD. The enzyme displayed Km and kcat values...
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