Properties of Purified β-Amylase from Satoimo (Taro Roots)

Abstract

β-Amylase of raw taro roots (Colocasia antiquorum Schott var. esculenta Engler) was purified to elucidate its properties.
Some characteristics of the β-amylase obtained were as follows : optimum pH 5.0, the stable range pH 5-7, optimum temperature 55°C, K_m 0.95 %, molecular weight 60, 000-61, 000, isoelectric point 6.8. The enzyme was suggested to have SH group. Several inhibitors were studied. These properties were discussed in comparison to 43-amylase of various origins.