Functional expression of miraculin, a taste-modifying protein in Escherichia coli.
Miraculin isolated from red berries of Richadella dulcifica, a native shrub of West Africa, has the unusual property of modifying a sour taste into a sweet one. This homodimer protein consists of two glycosylated polypeptides that are cross-linked by a disulfide bond. Recently, functional expression of miraculin was reported in host cells with the ability to glycosylate proteins, such as lettuce, tomato and the microbe Aspergillus oryzae, but not Escherichia coli. Thus, a question remains as to whether glycosylation of miraculin is essential for its taste-modifying properties. Here we show that recombinant miraculin expressed in E. coli has taste-modifying properties as a homodimer, not as a monomer, indicating that glycosylation is not essential for the taste-modifying property.
Matsuyama
Tomomi
T
Department of Food Science and Nutrition, Nara Women's University, Nara, 630-8506, Japan.
Satoh
Makiko
M
Nakata
Rieko
R
Aoyama
Takashi
T
Inoue
Hiroyasu
H
D001120:Arginine / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D005638:Fruit / Q000737:chemistry; D010940:Plant Proteins / Q000302:isolation & purification / Q000378:metabolism*; D055503:Protein Multimerization; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification; D012995:Solubility; D013649:Taste
D010940:Plant Proteins; D011994:Recombinant Proteins; D001120:Arginine