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학술저널
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Sarker, Goutam Kumar (Department of Biochemistry and Molecular Biology, University of Rajshahi) Hasan, Sohel (Department of Biochemistry and Molecular Biology, University of Rajshahi) Nikkon, Farjana (Department of Biochemistry and Molecular Biology, University of Rajshahi) Mosaddik, Ashik (Faculty of Biotechnology, Jeju National University) Sana, Niranjan Kumar (Department of Biochemistry and Molecular Biology, University of Rajshahi) Rahman, Habibur (Department of Biochemistry and Molecular Biology, University of Rajshahi) Park, Sang-Gyu (Division of Life & Environmental Science, Daegu University) Lee, Dong-Sun (Faculty of Biotechnology, Jeju National University) Cho, So-Mi Kim (Faculty of Biotechnology, Jeju National University)
저널정보
한국응용생명화학회 Applied Biological Chemistry Applied Biological Chemistry 제53권 제1호
발행연도
2010.1
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8 - 14 (7page)

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Purification, characterization and biochemical properties of $\alpha$-amylase from post harvest Bangladeshi Potato (Solanum tuberosum L.) were investigated. The $\alpha$-amylase was purified by successive chromatography on DEAE and CM-cellulose columns with a yield of 24.24%. SDSPAGE showed a molecular weight of 44 kDa for the enzyme that contain 2.8% sugar. The enzyme lost total activity in the presence of the chelating agent EDTA, confirming it was an $\alpha$-type amylase. The enzyme displayed optimum activity at pH 7.2 and $37^{\circ}C$, with an apparent Km value of 0.26% using starch as its substrate. The enzyme was strongly inhibited by $Cu^{2+},\;Fe^{2+}$ and $Zn^{2+}$; moderately by $Li^+,\;Hg^+$ and $Cd^{2+}$; and slightly by $Ag^+,\;K^+,\;Mn^{2+}$ and $Mg^{2+}$. Conversely, $Fe%{3+}$ and $Na^+$ appreciably enhanced activity, while adding calcium ion nearly doubled enzyme activity. In addition, the activity of $\alpha$-amylase gradually decreased with increasing concentrations of urea. Thus, potato $\alpha$-amylase is an attractive target for study to better understand the structure-function relationships of $\alpha$-amylases.

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