Abstract
The first extremely thermostable β-amylase from Clostridium thermosulfurogenes was partially purified to 98-fold. It readily and strongly adsorbed onto raw starch. p-Chloromercuribenzoate treated β-amylase lost its activity toward raw or gelatinized starch but the ability to be adsorbed onto raw starch was preserved. Adsorbed β-amylase was gradually released from starch in the liquid phase during hydrolysis at 75°C. The degradation of raw starch by β-amylase was greatly stimulated by pullulanase addition. The optimum pH for raw starch hydrolysis by β-amylase was pH 4.5 to 5.5, whereas that of soluble starch hydrolysis was at pH 5.5 to 6.0. The optimum temperature for hydrolysis of gelatinized starch was 75°C. β-Amylase did not require any metal ions for activity. Raw starch adsorbed β-amylase and soluble β-amylase showed similar rates of hydrolysis in reaction mixtures. The oxygen insensitive β-amylase from C. thermosulfurogenes displayed industrial utility for the production of high maltose syrups from raw or soluble starch at 75°C.
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