Developments in biotechnological production of sweet proteins.
Most proteins are tasteless and flavorless, while some proteins elicit a sweet-taste response on the human palate. Six proteins, thaumatin, monellin, mabinlin, brazzein, egg lysozyme, and neoculin (previously considered as curculin) have been identified as sweet-tasting proteins. However, no common features among them have been observed. Herein, recent advances in the research of sweet-tasting proteins and the production of such proteins by biotechnological approaches are reviewed. Information on the structure-sweetness relationship for these proteins would help not only in the clarification of the mechanism of interaction of sweet-tasting proteins with their receptors, but also in the design of more effective low-calorie sweeteners.
Masuda
Tetsuya
T
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.
Kitabatake
Naofumi
N
D001419:Bacteria / Q000378:metabolism*; D001709:Biotechnology; D005658:Fungi / Q000378:metabolism*; D010940:Plant Proteins / Q000096:biosynthesis; D030821:Plants, Genetically Modified; D011994:Recombinant Proteins / Q000096:biosynthesis*; D013329:Structure-Activity Relationship; D013549:Sweetening Agents
D010940:Plant Proteins; D011994:Recombinant Proteins; D013549:Sweetening Agents; C090521:brazzein protein, Pentadiplandra brazzeana; C002541:monellin protein, Dioscoreophyllum cumminsii; C003427:thaumatin protein, plant