Purification and characterization of alkali-stable beta-amylase from Chinese yam (Nagaimo) tuber
2006
Chiba, Y.(Fukushima Univ. (Japan). Faculty of Human Development and Culture) | Kuwashima, T.
An alkali-stable beta-amylase was purified from Nagaimo, a cultivar of yam (Dioscorea opposita Thunb.) by hexadecyltrimethylammonium bromide treatment, ammonium sulfate fractionation, and two-step column chromatographic procedures on alpha-CD-Sepharose CL-4B and DEAE-Sephacel. Analysis by SDS-PAGE revealed the enzyme to be a monomeric protein with a 56 kDa molecular mass. This enzyme was stable for pH 4.0-12.0 at 4 deg C for 24 h. During two months, its activity remained about 40% at pH 9.5, but it fell below 20% at pH 5.0. Other properties such as optimum pH (5.6) and molecular mass resembled those of previously reported beta-amylases. Thermal stability of this enzyme was not very high, either. From these results, this enzyme appears to be a good model for studying beta-amylase stability.
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