Functional Expression of Miraculin, a Taste-Modifying Protein in Escherichia Coli. Matsuyama, T., Satoh, M., Nakata, R., Aoyama, T., & Inoue, H. The Journal of Biochemistry, 145(4):445–450, April, 2009. ![Functional Expression of Miraculin, a Taste-Modifying Protein in Escherichia Coli [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{matsuyama_functional_2009,
title = {Functional {Expression} of {Miraculin}, a {Taste}-{Modifying} {Protein} in {Escherichia} {Coli}},
volume = {145},
issn = {0021-924X},
url = {https://doi.org/10.1093/jb/mvn184},
doi = {10.1093/jb/mvn184},
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.},
number = {4},
urldate = {2021-04-04},
journal = {The Journal of Biochemistry},
author = {Matsuyama, Tomomi and Satoh, Makiko and Nakata, Rieko and Aoyama, Takashi and Inoue, Hiroyasu},
month = apr,
year = {2009},
pages = {445--450},
}
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