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Research Support, Non-U.S. Gov't
- Recombinant Expression and Purification of Functional XorII, a Restriction Endonuclease from Xanthomonas oryzae pv. oryzae
- Dong Kyu Hwang 1, Jae-Yong Cho 2, Young Kee Chae 1
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Journal of Microbiology 2007;45(2):175-178
DOI: https://doi.org/2515 [pii]
1Department of Chemistry, Sejong University, Seoul 143-747, Republic of Korea, 2Department of Bioindustry and Technology, Sangji University, Gangwon-Do 220-702, Republic of Korea1Department of Chemistry, Sejong University, Seoul 143-747, Republic of Korea, 2Department of Bioindustry and Technology, Sangji University, Gangwon-Do 220-702, Republic of Korea
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Corresponding author:
Young Kee Chae , Tel: 82-2-3408-3748,
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Abstract
An endonuclease from Xanthomonas oryzae pathovar oryzae KACC 10331, XorII, was recombinantly produced in Escherichia coli using a T7 system. XorII was purified using a combination of ion exchange and immobilized metal affinity chromatography (IMAC). An optimized washing protocol was carried out on an IMAC in order to obtain a high purity product. The final amount of purified XorII was approximately 2.5 mg/L of LB medium. The purified recombinant XorII was functional and showed the same cleavage pattern as PvuI. The enzyme activity tested the highest at 25°C in 50 mM NaCl, 10 mM Tris-HCl, 10 mM MgCl2, and 1 mM dithiothreitol at a pH of 7.9.
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