An efficient purification with a high recovery of the inulin fructotransferase of Arthrobacter sp. A-6 from recombinant Escherichia coli |
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Authors: | Hwa-Young Kim Il-Hwan Kim Yong-Jin Choi |
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Institution: | (1) Graduate School of Biotechnology, Korea University, Seoul, 136-701, Korea;(2) Seo-Do Chemical Co., Ltd, 449-3, Moknae-Dong, Ansan, Kyonggi-Do, 425-100, Korea |
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Abstract: | Inulin fructotransferase (IFTase, EC 2.4.1.93) of Arthrobacter sp. A-6 was purified from a cell extract of the recombinant Escherichia coli DH5 /pDFE cells carrying the IFTase gene using heat treatment followed by gel filtration. The enzyme was purified 45-fold to apparent homogeneity with a recovery of 79%. SDS-PAGE yielded a single protein band of M
r 46.5 kDa. The recombinant IFTase had a similar thermostability as the original enzyme from Arthrobacter sp. A-6. |
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Keywords: | difructofuranose fructotransferase inulin recombinant Escherichia coli |
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