| Title | Purification and Characterization of α-amylase from Aspergillus sp. JP-1 |
|---|---|
| Author | Park, Hyung Nam · Yoo, Jin Cheol¹· Yang, Young Ki * |
| Address | Department of Genetic Engineering; ¹Department of Pharmacy, Chosun University |
| Bibliography | Journal of Microbiology, 33(1),80-84, 1995, |
| DOI | |
| Key Words | Aspergillus, α-amylase, purification |
| Abstract | The α-amylase was purified from Aspergillus sp. JP-1 and some enzyme characteristics were studied. The enzyme waw approzimately purified 80-fold and an overall yield was 16.5% from the culture medium by ammonium sulfate fractionation, Sephadex G-150 gel permeation chromatography, and DEAE-Sephadex A-50 ion exchange column chromatography in order. The molecular weight of the purified α-amylase has been estimated to be 56 KDa on SDS-polyacrulamide gel electrophoresis and Sephadex G-150 chromatography. The purigied enzyme functions optimally at pH5.5 and 40℃, respectively. The Km value for soluble starch was 2.5 mg/ml. The enzymatic activity increased in the presence of Ca^2+, Co^2+, EDTA, Mg^2+, Mn^2+ and Zn^2+ and was inhibited by adding Cu^2+, Fe^2+, and Ni^2+. |
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