With sugarplums dancing in my head, I thought a blog about something sweet, or in this case Cweet™, would be perfect. The smell of holiday cookies makes my mouth water, but then the realization of how much sugar is in those cookies makes me take a moment to question whether or not I really want to indulge. Scenarios such as this are why food manufacturing companies are constantly on the look out for new low calorie or, preferably, no calorie sweeteners. An up-and-comer in this growing industry is Natur Research Ingredients of Los Angeles who announced they will be manufacturing Cweet™ Natural Intense Sweetener, which is derived from the fruit of a West African tropical plant named Pentadiplandra brazzeana Baillon. The extract from the plant is called brazzein and is
"2000 times sweeter than sucrose when compared to a 2% sucrose solution in water and 500 times sweeter compared to 10% sugar solution. However, it has a taste closer to sucrose itself than other sweet proteins, such as thaumatin, is soluble in water and its sweetness is maintained even at 80 Celsius, which is important for foods that must be pasteurised, for instance. Wisconsin's Fariba Assadi-Porter uses NMR to study the structure-function relationships in brazzein and its analogues in order to understand precisely why this compound so stimulates our sweet receptors. Stable-isotope-assisted multinuclear NMR is the key that unlocks detailed chemical and structural information at the atomic level when the compound is present in living cells and interacting with the receptor. The team's current model of the binding of brazzein to the sweet receptor, suggests that the 54-amino acid protein chain binds at several points to the receptor. The sweet proteins do not share the same chemical properties as sugars like sucrose. In fact, these proteins do not interact with the same binding sites as sugars. "What makes these proteins sweet is far more complex than small sweeteners like sucrose, aspartame, etc," Assadi-Porter told SpectroscopyNOW, "There are many factors that dictate sweetness, such as the three-dimensional fold and large positive charges." She and her colleagues are now attempting to understand the detailed structural and chemical properties that are important for the sweetness of brazzein and its interaction with the sweet receptor." ("Sweet Structure Producer", spectroscopynow.com)
The complexity of the structure with the simplicity of the pleasure of something so sweet is amazing and even more intriguing is that brazzein tastes sweet only to old world monkeys and humans. I, for one, am thankful to be able to enjoy all the sweets in my life. May you all have a Happy Holiday Season and focus on all the sweets in your life.
The above excerpt was taken from
this article in
spectroscopynow.com. For more information, please refer to that article as well as the
Wisconsin Alumni Research Foundation.
