Improved sweetener available for licensing.

The consumption of sugar, the most widely used sweetener, can lead to significant problems such as undesirable weight gain caused by its high-calorie content. Moreover, most other sweeteners either have unwanted side effects or temporal sweetness profiles that do not adequately match those of sugar.

Brazzein is a natural sugar substitute which is up to 1000 times sweeter than sucrose. Brazzein is isolated from the West African fruit of the Ballion plant, Pentadiplandra brazzeana. It is a naturally occurring sweet protein and an enzyme that was first isolated as a sugar alternative by researchers at the University of Wisconsin. It has been licensed commercially.

More recently, the university is looking to license new variants of the natural brazzein protein that offer better sweetness haracteristics than other brazzein variants and wild brazzein. Scientists are creating these variants by modifying the amino acid sequence of brazzein. Replacing a single amino acid with either alanine or arginine, or adding alanine or arginine to the amino acid sequence, significantly improved the sweetness profiles of the variants.

In animal tests, besides producing a stronger response, the variants elicited a nerve fiber profile much closer to that of sucrose than did wild brazzein or other brazzein variants. Consumers also reported the taste of the new variants was purely sweet, with no sourness, saltiness or bitterness.

The new variants have temporal sweetness profiles much closer to sucrose than either wild-type brazzein or previous brazzein variants. The new variants are three to four times sweeter than wild brazzein, which itself is many times sweeter than sucrose. The sweetener is stable when exposed to elevated temperatures for long periods of time.

Patent. 7,153,535. Protein sweetener. Issued Dec. 26, 2006. Inventors: Zheyuan Jin, et al. Assigned to Wisconsin Alumni Research Foundation, Madison, WI. This patent covers sweet proteins that are variants of brazzein, and nucleotide sequences capable of expressing them. Through a replacement of a particular amino acid in the naturally occurring brazzein sequence, the taste profile and sweetness strength can be improved.

Further information. Goran Hellekant, Department of Animal Health and Biomedical Sciences, School of Veterinary Medicine, University of Wisconsin, 1656 Linden Dr., Madison, WI 53706; phone: 608-262-3177; fax: 608-262-7420; email: hellekant@svm.vetmed.wisc.edu. Licensing: Paul Pucci, Licensing Associate, Wisconsin Alumni Research Foundation, 614 Walnut St., Madison, WI 53726; phone: 608-262-4924; fax: 608-263-1064; email: ppucci@warf.org.

In this report ... Consider licensing new variants of a natural protein that offer improved sweetness characteristics. Scientists are creating these variants by modifying amino acid sequences. Look into creating new foods from an edible byproduct of ethanol production. Researchers are working on many fronts to find new uses for the growing supply of this byproduct as ethanol production continues to grow. Then see what effect individual amino acids have on the thermodynamics of flavor adsorption. The physical and chemical adsorption of flavor compounds onto food matrices facilitates flavor retention, balanced release and quality.