ArticleScientific reports2016
A Hypersweet Protein: Removal of The Specific Negative Charge at Asp21 Enhances Thaumatin Sweetness.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structural and Energetic Determinants of Sweet Protein Recognition: Mechanistic Insights into Thaumatin Binding to the Human T1R2/T1R3 Receptor.International journal of molecular sciences · 2026Article
- A Super Stable Mutant of the Plant Protein Monellin Endowed with Enhanced Sweetness.Life (Basel, Switzerland) · 2021Article
- Current Progress in Understanding the Structure and Function of Sweet Taste Receptor.Journal of molecular neuroscience : MN · 2021Review
- New Insight Into the Structure-Activity Relationship of Sweet-Tasting Proteins: Protein Sector and Its Role for Sweet Properties.Frontiers in nutrition · 2021Article
- Contextualized genome-scale model unveils high-order metabolic effects of the specific growth rate and oxygenation level in recombinantMetabolic engineering communications · 2019Article
- Metabolic Effects of the Sweet Protein MNEI as a Sweetener in Drinking Water. A Pilot Study of a High Fat Dietary Regimen in a Rodent Model.Nutrients · 2019Article
- High-level production of single chain monellin mutants with enhanced sweetness and stability in tobacco chloroplasts.Planta · 2018Article
- Transcriptome and miRNA analyses of the response to Corynespora cassiicola in cucumber.Scientific reports · 2018Article
- Positive Charges on the Surface of Thaumatin Are Crucial for the Multi-Point Interaction with the Sweet Receptor.Frontiers in molecular biosciences · 2018Article
- Sweeter and stronger: enhancing sweetness and stability of the single chain monellin MNEI through molecular design.Scientific reports · 2016Article
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8 authors.
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Abstract
Thaumatin is an intensely sweet-tasting protein that elicits sweet taste at a concentration of 50 nM, a value 100,000 times larger than that of sucrose on a molar basis. Here we attempted to produce a protein with enhanced sweetness by removing negative charges on the interacting side of thaumatin with the taste receptor. We obtained a D21N mutant which, with a threshold value 31 nM is much sweeter than wild type thaumatin and, together with the Y65R mutant of single chain monellin, one of the two sweetest proteins known so far. The complex model between the T1R2-T1R3 sweet receptor and thaumatin, derived from tethered docking in the framework of the wedge model, confirmed that each of the positively charged residues critical for sweetness is close to a receptor residue of opposite charge to yield optimal electrostatic interaction. Furthermore, the distance between D21 and its possible counterpart D433 (located on the T1R2 protomer of the receptor) is safely large to avoid electrostatic repulsion but, at the same time, amenable to a closer approach if D21 is mutated into the corresponding asparagine. These findings clearly confirm the importance of electrostatic potentials in the interaction of thaumatin with the sweet receptor.
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