12 January - 20 June 2016

Controlling the taste receptor accessible structure of rebaudioside A via binding to bovine serum albumin

18 November 2015

Steviol glycosides, extracted from Stevia plants, are increasingly popular as a sweetener in a wide variety of products, as consumers demand ‘natural’ alternatives to both plain sugar and artificial sweeteners like aspartame. However, they have their downsides – a bitter aftertaste which can ruin the sensory experience of a sweetened food or drink and is a challenge to overcome. Existing methods for mediating this effect are inefficient and costly to implement, using complex reactions (a concern for safety and the perceived ‘natural’ origin of the product) producing poor yield, or relying heavily on other flavour modifiers.

Research published by workers at Cornell University in Food Chemistry offers a potential new approach, which depends not on modifying the compound or masking it with other flavour enhancers, but on deactivation of the bitter component. Rebaudioside A (Reb A) is the glycoside part providing the sweetness in steviol glycosides, but is also responsible for bitter flavours. Researchers successfully demonstrated that the bitter region can be bound by BSA (Bovine Serum Albumin) in a specific and hydrophobic interaction (similar to those encountered by BSA in its natural environment, binding large hydrophobic molecules in the blood). A further experiment using orange juice showed that this interaction is specific and stable even in the complex matrix of a foodstuff – which may in turn mean that Reb A could be routinely modified in the future, becoming a better sweetener and a more attractive prospect for consumers.

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