Studies on flavored peptides. Part III. Role of the hydrophobic amino acid residue in the bitterness of peptides.
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- ISHIBASHI Norio
- Morinaga Milk Industry Co., Ltd. Nutritional Science Laboratory
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- ONO Ichiro
- Department of Fermentation Technology, Faculty of Engineering, Hiroshima University
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- KATO Kuniki
- Department of Fermentation Technology, Faculty of Engineering, Hiroshima University
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- SHIGENAGA Toshiaki
- Department of Fermentation Technology, Faculty of Engineering, Hiroshima University
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- SHINODA Ichizo
- Department of Fermentation Technology, Faculty of Engineering, Hiroshima University
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- OKAI Hideo
- Department of Fermentation Technology, Faculty of Engineering, Hiroshima University
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- FUKUI Sakuzo
- Department of Fermentation Technology, Faculty of Engineering, Hiroshima University
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In order to investigate the role of the side chain of amino acids in the bitterness in peptide, some oilgopeptides containing glycine, alanine, aminobutyric acid, valine, isoleucine, norvaline (n-Val) and norleucine (n-Leu) were synthesized and their tastes were evaluated. For the bitter taste to be exhibited, the side chain skeleton of the amino acid should consist of at least three carbons. The peptides consisting of amino acids having a side chain of less than three carbons did not exhibit bitterness, while the peptides consisting of amino acids having a side chain of more than three carbons did exhibit bitterness. Valine exhibited an intermediate feature, the taste of valine peptides varying dependent upon the structure. The difference of the branching structure in side chains was less concerned with peptide bitterness.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 52 (1), 91-94, 1988
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681445265152
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- NII論文ID
- 110006323427
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- NII書誌ID
- AA00515312
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- COI
- 1:CAS:528:DyaL1cXhvVChsbc%3D
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- ISSN
- 18811280
- 00021369
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- 本文言語コード
- en
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- データソース種別
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- JaLC
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- 使用不可