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|Title:||Isolation, characterization and potential application of deoxyribonuclease-free phosphatase from cassava leaves||Authors:||Tham, S.C.
|Issue Date:||Feb-2006||Citation:||Tham, S.C.,Lim, S.H.,Yeoh, H.H. (2006-02). Isolation, characterization and potential application of deoxyribonuclease-free phosphatase from cassava leaves. Acta Horticulturae 703 : 263-267. ScholarBank@NUS Repository.||Abstract:||A deoxyribonuclease-free acid phosphatase from cassava leaves was prepared by ammonium sulfate precipitation, chromatofocusing and hydrophobic interaction chromatography with phenyl Sepharose. The enzyme was purified 36-fold and had a specific activity of 16 U/ mg protein. The enzyme preparation revealed a major phosphatase band of 77 kDa and three minor activity bands. The pH and temperature optima for enzyme activity were 5.2 and 60°C, respectively. The enzyme was inactivated by heating at 80°C for 15 minutes and could be stored at - 20°C for up to two months. The enzyme exhibited broad substrate specificity and had a Km, (p-nitrophenyl phosphate) value of 1.7 mM. It was strongly inhibited by zinc and copper ions, molybdate and arsenate. Aluminium ions, ferrous ions, dithiothreitol and mercaptoethanol stimulated enzyme activity within 0.5-5.0 mM range. The enzyme partially dephosphorylated linearized pUC18 plasmid despite being an acid phosphatase and showed potential application as a substitute for alkaline phosphatase in the ELISA procedure.||Source Title:||Acta Horticulturae||URI:||http://scholarbank.nus.edu.sg/handle/10635/102217||ISBN:||9066053879||ISSN:||05677572|
|Appears in Collections:||Staff Publications|
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