Critical regions for the sweetness of brazzein 1

FEBS Letters

Jin, Zheyuan²  Markley, John L¹  Hellekant, Göran²  Aceti, David J¹  Assadi-Porter, Fariba M¹  Danilova, Vicktoria² 

[1] Department of Biochemistry, University of Wisconsin–Madison, Madison, WI 53706, USA;Department of Animal Health and Biomedical Sciences, University of Wisconsin–Madison, Madison, WI 53706, USA

关键词: Brazzein;    Sweet protein;    Mutagenesis;    Sweetness determinant;    Sweetness evaluation;    Taste;    CNBr;    cyanogen bromide;    ddH2O;    doubly deionized water;    MALDI;    matrix-assisted laser desorption/ionization;    NMR;    nuclear magnetic resonance;    pGlu;    pyroglutamic acid;    SCM;    single-chain monellin;    SNase;    staphylococcal nuclease;    WT;    wild type;    WT brazzein;    recombinant des-pGlu1 brazzein;   

DOI  :  10.1016/S0014-5793(03)00383-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown