Solid-phase Synthesis and Structure-Taste Relationships of Analogs of the Sweet Protein Monellin
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概要
- 論文の詳細を見る
The amino acid residues within potential active sites of monellin were replaced. The replacement of Ile^<B6>, Asp^<B7>, or Ile^<B8> by different amino acids resulted in a complete or marked loss of sweetness, while the replacement of Tyr^<A13> or Asp^<A16> by other amino acids did not substantially reduce the sweetness. The replacement of each Lys residue by L-2-aminohexanoic acid significantly reduced the sweetness potency, but did not completely remove the sweetness. An analysis of synthetic analogs by CD showed that the major structural features of monellin were not significantly altered. These findings suggest that Ile^<B6>, Asp^<B7>, and Ile^<B8> are responsible for eliciting a sweet taste, and that one or more basic residues may also be important for sweetness.
- 社団法人日本農芸化学会の論文
- 1994-08-23
著者
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Nio Noriki
Central Research Laboratories, Ajinomoto Co., Inc.
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Ariyoshi Yasuo
Central Research Laboratories, Ajinomoto Co., Inc.
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Nio N
Ajinomoto Co. Inc. Kanagawa Jpn
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Ariyoshi Y
Ajinomoto Co. Inc. Kawasaki Jpn
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Ariyoshi Yasuo
Central Research Laboratories Ajinomoto Co. Inc
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Kohmura M
Ajinomoto Co. Inc. Kawasaki Jpn
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Kohmura Masanori
Central Research Laboratories, Ajinomoto Co., Inc.
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Kohmura Masanori
Central Research Laboratories Ajinomoto Co. Inc.
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