The demand for non-calorigenic protein-based sweeteners with favorable taste properties is high. Most proteins are tasteless and flavorless, while some proteins elicit a sweet-taste response on the human palate.1 Seven sweet-taste proteins derived from a variety of plants (or rarely from animals) were identified as eliciting a sweet-taste response: thaumatin; monellin; mabinlin;brazzein; neoculin; miraculin; egg white lysozyme. Among them, brazzein possessed better pH and thermal stabilities and a pleasant sweet taste profile. Brazzein was isolated from the fruit of the West African Pentadiplandra brazzeana Baillon plant.2 It is a single-chain polypeptide consisting of 54 amino acid residues, with a correspondi... More
The demand for non-calorigenic protein-based sweeteners with favorable taste properties is high. Most proteins are tasteless and flavorless, while some proteins elicit a sweet-taste response on the human palate.1 Seven sweet-taste proteins derived from a variety of plants (or rarely from animals) were identified as eliciting a sweet-taste response: thaumatin; monellin; mabinlin;brazzein; neoculin; miraculin; egg white lysozyme. Among them, brazzein possessed better pH and thermal stabilities and a pleasant sweet taste profile. Brazzein was isolated from the fruit of the West African Pentadiplandra brazzeana Baillon plant.2 It is a single-chain polypeptide consisting of 54 amino acid residues, with a corresponding molecular mass of approximately 6.5 kDa. Brazzein is heat-stable, with its sweetness remaining after heating at 98 oC for 2 h and 80 oC for 4.5 h at a pH range of 2.5 - 8. This stability may be due to four intramolecular disulfide bonds and the absence of no-free sulfhydryl groups within the molecule. Brazzein water solubility is at least 50 mg/mL. From the point of view of its sweetness, heat stability,high water solubility, and minimum molecular weight, brazzein is currently the superior protein sweetener.
