Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities
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- 作者：Suzuki ; Maiko ; Kurimoto ; Eiji ; Nirasawa ; Satoru ; Masuda ; Yutaka ; Hori ; Kouichi ; Kurihara ; Yoshie ; et. al.
- 关键词：CD ; circular dichroism ; DEAE ; diethylaminoethyl ; GSH ; glutathione reduced form ; GSSG ; glutathione oxidized form ; HPLC ; high-performance liquid chromatography ; MALDI ; matrix assisted laser desorption ionization ; PAGE ; polyacrylamide gel electrophoresis ; PC
- 刊名：FEBS Letters
- 出版年：2004
- 出版时间：August 27, 2004
- 年：2004
- 卷：573
- 期：1-3
- 页码：135-138
- 全文大小：113 K
文摘
Curculin from Curculigo latifolia is a unique sweet protein that exhibits both sweet-tasting and taste-modifying activities. We isolated a gene that encodes a novel protein highly homologous to curculin. Using cDNAs of the previously known curculin (designated as curculin1) and the novel curculin isoform (curculin2), we produced a panel of homodimeric and heterodimeric recombinant curculins by Escherichia coli expression systems. It was revealed that sweet-tasting and taste-modifying activities were exhibited solely by the heterodimer of curculin1 and curculin2.