Atomic structure of the sweet-tasting protein thaumatin I at pH 8.0 reveals the large disulfide-rich region in domain II to be sensitive to a pH change.

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Masuda, Tetsuya ; Ohta, Keisuke ; Mikami, Bunzo ; Kitabatake, Naofumi ; Tani, Fumito (2012)
  • Publisher: Elsevier Inc.
  • Journal: Biochemical and biophysical research communications, volume 419, issue 1, pages 72-76 (issn: 0006-291X)
  • Subject: Thaumatin | Heat | Hydrogen-atoms | Alkaline conditions | SHELXL | Sweet-tasting protein
    mesheuropmc: food and beverages

Thaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at 50 nM. Although the sweetness remains when thaumatin is heated at 80 °C for 4h under acid conditions, it rapidly declines when heating at a pH above 6.5. To clarify the structural difference a... View more
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