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dc.contributor.authorHuang, CYen_US
dc.contributor.authorYang, YSen_US
dc.date.accessioned2014-12-08T15:40:00Z-
dc.date.available2014-12-08T15:40:00Z-
dc.date.issued2003-12-12en_US
dc.identifier.issn0006-291Xen_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.bbrc.2003.10.151en_US
dc.identifier.urihttp://hdl.handle.net/11536/27323-
dc.description.abstractIn this paper we report the first comparative study of cold-adapted imidase (EC 3.5.2.2) 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 degreesC or lower) conditions but less stable at elevated temperatures (40 degreesC 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. (C) 2003 Elsevier Inc. All rights reserved.en_US
dc.language.isoen_USen_US
dc.titleA novel cold-adapted imidase from fish Oreochromis niloticus that catalyzes hydrolysis of maleimideen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.bbrc.2003.10.151en_US
dc.identifier.journalBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONSen_US
dc.citation.volume312en_US
dc.citation.issue2en_US
dc.citation.spage467en_US
dc.citation.epage472en_US
dc.contributor.department生醫工程研究所zh_TW
dc.contributor.departmentInstitute of Biomedical Engineeringen_US
dc.identifier.wosnumberWOS:000186987000029-
dc.citation.woscount8-
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