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자료유형
학술저널
저자정보
Kang, Han-Chul (Department of Molecular Physiology, National Institute of Agricultural Biotechnology, Rural Development Administration) Kim, Jong-Bum (Department of Molecular Physiology, National Institute of Agricultural Biotechnology, Rural Development Administration) Lee, Hak-Sun (Department of Molecular Physiology, National Institute of Agricultural Biotechnology, Rural Development Administration) Cho, Kang-Jin (Department of Molecular Physiology, National Institute of Agricultural Biotechnology, Rural Development Administration)
저널정보
한국응용생명화학회 Journal of applied biological chemistry Journal of applied biological chemistry 제51권 제3호
발행연도
2008.1
수록면
95 - 101 (7page)

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The gene encoding a putative esterase of Xanthomonas oryzae pv. oryzae was cloned using PCR technique. The gene was expressed with His6 tag in E. coli. One-step purification of the recombinant esterase with Ni-NTA resin resulted in one band by SDS-PAGE analysis. The purified enzyme showed a molecular weight of 30 kDa, as expected, therefore the enzyme was a mononer. The enzyme was the most active toward p-nitrophenyl (p-NP) acetate and p-NP-butyrate to a lesser extent. However, the enzyme could not hydrolyze p-NP-myristate, palmitate, and stearate. Therefore, the enzyme is considered as an esterase, very different from lipase. The purified esterase had optimal pH at around 8.0 and was stable in a broad range of pH values. The optimal temperature ranged from 30 to $40^{\circ}C$, and the residual activity observed after heat treatment at $55^{\circ}C$ for 20 min was 72 % of the initial activity. The activity was inhibited by the presence of copper and cobalt ions.

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