Recent developments in the characterization and biotechnological production of sweet-tasting proteins.
The state of the art regarding the six known sweet-tasting proteins (thaumatin, monellin, mabinlin, pentadin, brazzein and curculin) and the taste-modifying protein miraculin is reviewed. Their biochemical properties, molecular genetics and biotechnological production are assessed. All of these proteins have been isolated from plants that grow in tropical rainforests. They share no sequence homology or structural similarities. Nonetheless, one of them, thaumatin, shares extensive homology with certain non-sweet proteins found in other plants. The potential industrial applications of the sweet-tasting proteins are also discussed, placing special emphasis on the barriers that a recombinant product of these characteristics will have to overcome before it reaches the market.
Faus
I
I
Laboratory of Biotechnology, URIACH GROUP, Sant Fost de Campsentelles, Barcelona, Spain. urquima@uriach.com
D000596:Amino Acids; D005638:Fruit / Q000737:chemistry*; D015870:Gene Expression; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000378:metabolism; D017385:Sequence Homology; D013549:Sweetening Agents / Q000737:chemistry*
D000596:Amino Acids; D010940:Plant Proteins; D011994:Recombinant Proteins; D013549:Sweetening Agents