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<p>Changes in the colloidal state of sweet proteins may affect their sweetness during processing and in the oral environment. This study examined the effects of pH, temperature, NaCl, and artificial saliva on thaumatin. Particle size, solubility, turbidity, spectroscopic properties, electronic tongue responses, and sensory scores were analyzed to assess aggregation behavior and sweetness changes. Close to pH 8.0 and after the addition of NaCl, the aggregation of thaumatin was the most obvious, and the content of soluble protein was reduced in both cases. Heating at 55–90&#xa0;°C increased the particle size to 107–173&#xa0;nm, but the secondary structure only changed to a limited extent. In contrast, pH 11.0 and NaCl had broader effects on the colloidal properties and conformation of thaumatin. The sensory sweetness score was 7.94 in CK, but decreased to 3.72 after treatment at pH 11.0 and to 3.78 after treatment with 0.1&#xa0;mol/L NaCl. Artificial saliva also changed the particle-size distribution and was accompanied by a lower sweetness sensor response (SSR). This change may be related to interactions between thaumatin and salivary components. These results showed that the dispersion state of thaumatin was related to its sweetness. The stability and sweetness of thaumatin can be maintained during processing by preserving sufficient surface charge and limiting NaCl addition.</p>

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Effects of Environmental Stresses and Saliva on the Aggregation Behavior and Sweetness of Sweet-tasting Protein Thaumatin

  • 期刊论文

  • 发表日期：

    2026年7月28日

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  • Tingnan Song,
  • Ruoning Zhang,
  • Yanhui Zhang,
  • Yanxiang Gao,
  • Like Mao

摘要

Changes in the colloidal state of sweet proteins may affect their sweetness during processing and in the oral environment. This study examined the effects of pH, temperature, NaCl, and artificial saliva on thaumatin. Particle size, solubility, turbidity, spectroscopic properties, electronic tongue responses, and sensory scores were analyzed to assess aggregation behavior and sweetness changes. Close to pH 8.0 and after the addition of NaCl, the aggregation of thaumatin was the most obvious, and the content of soluble protein was reduced in both cases. Heating at 55–90 °C increased the particle size to 107–173 nm, but the secondary structure only changed to a limited extent. In contrast, pH 11.0 and NaCl had broader effects on the colloidal properties and conformation of thaumatin. The sensory sweetness score was 7.94 in CK, but decreased to 3.72 after treatment at pH 11.0 and to 3.78 after treatment with 0.1 mol/L NaCl. Artificial saliva also changed the particle-size distribution and was accompanied by a lower sweetness sensor response (SSR). This change may be related to interactions between thaumatin and salivary components. These results showed that the dispersion state of thaumatin was related to its sweetness. The stability and sweetness of thaumatin can be maintained during processing by preserving sufficient surface charge and limiting NaCl addition.