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Preparation of L-arabinose isomerase originated from Escherichia coli as a biocatalyst for D-tagatose production

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Abstract

l-Arabinose isomerase for tagatose production from recombinant Escherichia coli was partially purified 15-fold with a specific activity of 70 U mg−1 protein. The purified enzyme had a major band when it was subjected to SDS/PAGE. With the purified l-arabinose isomerase, 17.7 g tagatose l−1 was produced from 50 g galactose l−1 in 168 h which corresponds to a 34% equilibrium.

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Authors and Affiliations

  1. Basic Research Team, R&D Center, Tong Yang Confectionery Co., Seoul, 140-715, Korea

    Hoe-Jin Roh, Hoe-Jin Roh, Hoe-Jin Roh, Sang-Hyun Yoon, Sang-Hyun Yoon, Sang-Hyun Yoon, Pil Kim, Pil Kim & Pil Kim

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  1. Hoe-Jin Roh
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  2. Sang-Hyun Yoon
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  3. Pil Kim
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Roh, HJ., Yoon, SH. & Kim, P. Preparation of L-arabinose isomerase originated from Escherichia coli as a biocatalyst for D-tagatose production. Biotechnology Letters 22, 197–199 (2000). https://doi.org/10.1023/A:1005689030717

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  • DOI: https://doi.org/10.1023/A:1005689030717

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