Overexpression of the soluble form of chicken cystatin in Escherichia coli and its purification |
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Authors: | Chen G H Tang S J Chen C S Jiang S T |
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Institution: | Department of Food Science, National Taiwan Ocean University, Keelung. |
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Abstract: | A cDNA encoding chicken cystatin was cloned into the pET-23a(+) expression vector and then transformed into Escherichia coli AD494(DE3)pLysS expression host. An active soluble form of cystatin was expressed in the cytoplasm of E. coli induced by isopropyl beta-D-thiogalactopyranoside. The recombinant chicken cystatin was purified to electrophoretic homogeneity by a simple and rapid method involving heat treatment and Sephacryl S-100 gel filtration chromatography. The recombinant cystatin behaved as a thermal-stable protein and exhibited papain-like protease inhibition activity comparable to the natural chicken cystatin. |
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