Identification and Modulation of the Key Amino Acid Residue Responsible for the pH Sensitivity of Neoculin, a Taste-Modifying Protein
2011

Identifying the Key Amino Acid in Neoculin that Affects pH Sensitivity

Sample size: 10 publication 10 minutes Evidence: moderate

Author Information

Author(s): Nakajima Ken-ichiro, Yokoyama Kanako, Koizumi Taichi, Koizumi Ayako, Asakura Tomiko, Terada Tohru, Masuda Katsuyoshi, Ito Keisuke, Shimizu-Ibuka Akiko, Misaka Takumi, Abe Keiko

Primary Institution: The University of Tokyo

Hypothesis

Which histidine residues in neoculin are critical for its taste-modifying activity?

Conclusion

NBS His11 is identified as the primary pH sensor responsible for the taste-modifying activity of neoculin.

Supporting Evidence

  • Neoculin variants with substitutions other than His-to-Ala were analyzed to clarify the role of NBS position 11 in taste-modifying activity.
  • The study found that the aromatic character of the amino acid side chain is necessary for pH-dependent sweetness.
  • H11A(B) variant elicited a strong sweet taste under various pH conditions.

Takeaway

Neoculin is a protein that can make sour foods taste sweet, and scientists found that a specific part of it is key to this ability.

Methodology

The study involved creating various neoculin variants and testing their sweetness levels using cell-based assays and human sensory tests.

Limitations

The study primarily focused on a limited number of neoculin variants and their interactions with the sweet taste receptor.

Participant Demographics

Panel members were trained to evaluate sweetness intensity.

Statistical Information

P-Value

1.36 µM

Statistical Significance

p<0.05

Digital Object Identifier (DOI)

10.1371/journal.pone.0019448

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