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Studies on Purification and Characterization of Sweet Potato (Ipomoea Batatas) Cultivated in the Northern Part of Bangladesh

Enzyme activity was also determined from the Red sweet potato and white sweet potato. The activities of Amylase, Cellulase, Invertase, & protease were 0.093±0.01, 0.05±0.02, 0.062± 0.015, 0.043± 0.02, for Red while 0.088± 0.01, 0.073 ±0.02, 0.072 ±0.015 & 0.050± 0.02 for White sweet potato. Amylase was partially purified from the extract of sweet potato using DEAE cellulose column chromatography. On the purity checking and molecular weight determination on SDS-PAGE. The molecular weight was determined by SDS-PAGE to be 64±1 kDa. The partially purified amylase from sweet potato is β-type is confirmed by HgCl2.The optimum pH & temperatures of partially purified β-amylase were 7.5 and 55◦c respectively. Amylolytic activity of this enzyme is 105% and 55% for amylopectin and Amylase. This enzyme does not affect maltose and maltotetraose. Metallic ions like Fe3+, Mn2+, Mg2+, and EDTA increased amylase activity while other ions like Cu+2, Hg+2, Pb+2, and urea reduced the amylase activity. The study indicates the importance of β-amylase as a starch degrading enzyme. This enzyme showed less toxicity towards brine shrimp nauplii with the Lc50 value of 1970.288µg/ml. This enzyme did not show any antibacterial activity against Staphylococcus aureus, Escherichia coli, Salmonella enterica, Bacillus subtilis.

Keywords: Sweet potato, Ipomoea Batatas, Starch, Amylase, Protease.