Critical regions for the sweetness of brazzein.
Brazzein is a small, heat-stable, intensely sweet protein consisting of 54 amino acid residues. Based on the wild-type brazzein, 25 brazzein mutants have been produced to identify critical regions important for sweetness. To assess their sweetness, psychophysical experiments were carried out with 14 human subjects. First, the results suggest that residues 29-33 and 39-43, plus residue 36 between these stretches, as well as the C-terminus are involved in the sweetness of brazzein. Second, charge plays an important role in the interaction between brazzein and the sweet taste receptor.
Jin
Zheyuan
Z
Department of Animal Health and Biomedical Sciences, University of Wisconsin-Madison, 53706, USA.
Danilova
Vicktoria
V
Assadi-Porter
Fariba M
FM
Aceti
David J
DJ
Markley
John L
JL
Hellekant
Göran
G
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000378:metabolism; D005638:Fruit; D017343:Genes, Plant; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013053:Spectrophotometry; D013649:Taste; D014466:Ultraviolet Rays; D014867:Water / Q000737:chemistry
D010940:Plant Proteins; C090521:brazzein protein, Pentadiplandra brazzeana; D014867:Water