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Journal of Biochemistry Advance Access originally published online on January 3, 2009
Journal of Biochemistry 2009 145(4):445-450; 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; and 2Institute for Chemical Research, Kyoto University, Uji, 611-0011, Japan

*To whom correspondence should be addressed. Tel: +81-742-20-3458, Fax: +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: Escherichia coli, glycosylation, homodimer, miraculin, taste-modifying protein

Abbreviations: AAA, ATPase associated with a variety of cellular activities; PAGE, polyacrylamide gel electrophoresis; PCR, polymerase chain reaction; PMSF, phenylmethylsulfonyl fluoride; SDS, sodium dodecyl sulfate


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