Variation in Bitterness Potency When Introducing Gly-Gly Residue into Bitter Peptides |
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Authors: | Ichizo Shinoda Yasuharu Nosho Katsushige Kouge Norio Ishibashi Hideo Okai Kiyoshi Tatsumi |
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Affiliation: | 1. Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Shitami, Saijo-cho, Higashihiroshima 724, Japan;2. Snow Brand Milk Products Co., Ltd., 13 Honshio-cho, Shinjuku-ku, Tokyo 160, Japan |
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Abstract: | We previously reported that Gly-Gly-Arg-Pro and Arg-Pro-Gly-Gly, the derivatives of a bitter peptide Arg-Pro, had no bitterness although Gly-Arg-Pro and Arg-Pro-Gly had a bitter taste at the same level as that of Arg-Pro. To elucidate the mechanism of elimination of bitterness by the introduction of the Gly-Gly residues, we synthesized Gly-Gly derivatives of other bitter peptides such as Phe-Phe, Val-Val-Val, and Arg-Pro-Phe-Phe, and examined the effectiveness of Gly-Gly residues in eliminating bitterness. We suggest that, for Arg-Pro and Val-Val-Val, the Gly-Gly residue might prevent a hydrophobic group from binding to a taste receptor. |
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Keywords: | cytochrome c electrostatic interaction protein stability site-directed mutagenesis |
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