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Biochem Biophys Res Commun. 2003 Dec 12;312(2):467-72.

A novel cold-adapted imidase from fish Oreochromis niloticus that catalyzes hydrolysis of maleimide.

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Institute of Biochemical Engineering, College of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan, ROC.


In this paper we report the first comparative study of cold-adapted imidase (EC from the fish (Oreochromis niloticus) liver and its thermophilic counterparts taken from pig liver and Escherichia coli (overexpressed recombinant hydantoinase from Agrobacterium radiobacter NRRL B1). Approximately 6000-fold purification and a 40% yield of fish imidase activity were obtained through ammonium sulfate precipitation, octyl, chelating, DEAE, and hydroxyapatite chromatography. This cold-adapted imidase was characterized by a specific activity 10- to a 100-fold higher than those of its thermophilic counterparts below room temperature (25 degrees C or lower) conditions but less stable at elevated temperatures (40 degrees C or higher). A less organized helical structure (compared to those of pig liver and bacterial imidases) was observed by circular dichroism. Furthermore, maleimide was first identified as a novel substrate of all imidases examined, and confirmed by HPLC and NMR analysis. These results constituted a first study to discover a novel cold-adapted imidase with surprising high activity. These findings might be also helpful for industrial application of imidase.

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