Multiplicity and Preferential Inactivation by Proteolysis as to Raw Starch-digestibility of Bacterial α-Amylases(Microbiology & Fermentation Industry)

概要

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B. subtilis 65 α-amylase (MW 68,000) showed raw potato starch-digestibility and hydrolyzing ability toward low molecular weight substrates such as maltotriose (G3) γ-cyclodextrin (γCD) and p-nitrophenylmaltoside (PNP-G2). Kleistase α-amylase (MW 48,200), α-amylase purified from B. subtilis, showed strong raw corn starch-digestibility, but it was deficient in raw potato starch-digestibility and low molecular weight substrate-hydrolyzing ability. Liquefying α-amylase (MW45,000; purified from B. subtilis), which hardly digested raw starches, could not hydrolyze low molecular weight substrates. Raw starch-digesting α-amylase of B. subtilis 65 was converted to a raw starch-nondigesting form through the action of pronase. But, the pronase-digested α-amylase retained the hydrolyzing ability toward low molecular weight substrates. It is suggested that the characteristic region liberated by pronase is essential for digestion of raw starch by the amylase.
社団法人日本農芸化学会の論文
1989-03-23