標題: Purification of industrial hydantoinase in one chromatographic step without affinity tag
作者: Huang, CY
Chao, YP
Yang, YS
生物科技學系
Department of Biological Science and Technology
公開日期: 1-Jul-2003
摘要: Hydantoinase is used in industry as a biocatalyst for the production of optically pure D- or L-amino acids. Previously, homogeneous hydantoinase was obtained by multi-chromatographic purification procedures. Here, we reported a process that contained only a single chromatographic step to purify a recombinant hydantoinase to homogeneity. Hydantoinase from Agrobacterium radiobacter NRRL B11291 was expressed in Escherichia coli. The recombinant enzyme was purified following heat treatments, high concentration alcohol precipitation, and chelating Sephacel chromatography. The recombinant hydantoinase did not contain any affinity tags from the plasmid. This simplified procedure provided a convenient way to obtain hydantoinase in high yield (71%) and high purity. It should be very useful for further industrial application and for the study of the structure-function of hydantoinase. (C) 2003 Elsevier Science (USA). All rights reserved.
URI: http://dx.doi.org/10.1016/S1046-5928(03)00092-5
http://hdl.handle.net/11536/27742
ISSN: 1046-5928
DOI: 10.1016/S1046-5928(03)00092-5
期刊: PROTEIN EXPRESSION AND PURIFICATION
Volume: 30
Issue: 1
起始頁: 134
結束頁: 139
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