Recombinant curculin heterodimer exhibits taste-modifying and sweet-tasting activities.

Maiko Suzuki, Eiji Kurimoto, Satoru Nirasawa, Yutaka Masuda, Kouichi Hori, Yoshie Kurihara, Nobuhisa Shimba, Misako Kawai, Ei-Ichiro Suzuki, Koichi Kato

Journal: FEBS letters 2004;573(1-3):135-8

PMID: 15327988

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Abstract

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.

Address: Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.

DOI: 10.1016/j.febslet.2004.07.073

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MeSH Terms: Amino Acid Sequence, Circular Dichroism, Cloning, Molecular, Curculigo, Dimerization, Disulfides, Humans, Molecular Sequence Data, Oxidation-Reduction, Plant Proteins, Protein Structure, Quaternary, Protein Subunits, Recombinant Proteins, Sweetening Agents, Taste