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Journal of Biochemistry Advance Access published online on January 3, 2009
Journal of Biochemistry, doi:10.1093/jb/mvn184
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Functional expression of miraculin, a taste-modifying protein in Escherichia coli*

Tomomi Matsuyama1, Makiko Satoh1, Rieko Nakata1, Takashi Aoyama2 and Hiroyasu Inoue1,*

1Department of Food Science and Nutrition, Nara Women's University, Nara, 630-8506, JAPAN: and 2Institute for Chemical Research, Kyoto University, Uji, 611-0011, JAPAN

*To whom correspondence should be addressed: Prof. Hiroyasu Inoue: Department of Food Science and Nutrition, Nara Women's University, Nara, 630-8506, JAPAN. Fax: +81-742-20-3458. Tel: +81-742-20-3458. E-mail: inoue{at}cc.nara-wu.ac.jp

Received November 26, 2008; Accepted December 15, 2008


  Abstract

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.

Key Words: Miraculin, Taste-modifying protein, Glycosylation, Escherichia coli, Homodimer


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