Thaumatin, an intensely sweet-tasting protein, elicits a sweet taste sensation at 50 nM. Here the X-ray crystallographic structure of one of its variants, thaumatin II, was determined at a resolution of 1.27 Å. Overall structure of thaumatin II is similar to thaumatin I, but a slight shift of the Cα atom of G96 in thaumatin II was observed. Furthermore, the side chain of residue 67 in thaumatin...

matococcus daniellii Benth.i) The moleculaT mass of the protein is 22 kDa and the higher order structure of the protein is maintained by eight disulfide bridges.2・3) Thaumatin is the sweetest substance for man and is, on a molar basis, 100,OOO times sweeter than sucrose.i) Today, thaumatin is used commercially for its intense sweetness, taste masking, fiavor enhancement, and synergistic propert...

Grape thaumatin-like proteins (TLPs) play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. Different isoforms of TLPs have different hazing potential and aggregation behavior. Here we present the elucidation of the molecular structures of three grape TLPs that display different hazing potential. The three TLPs have very similar stru...

Two different strains, Aspergillus awamori TGDTh-4 and A. awamori TGP-3 overexpressing a synthetic gene encoding the plant sweet protein thaumatin, showed an unfolded protein response. To facilitate protein secretion, the chaperone BiPA gene was expressed in A. awamori under control of the strong constitutive promoter of the gpdA gene. A good correlation was observed between the level of the bi...

Thaumatin-like proteins (TLPs) are involved in the plant defense response against pathogens, and most of them exhibit antifungal activity. However, role TLPs pathogen-induced responses spruce is not fully understood. In this study, four TLP genes encoding thaumatin-like protein, designated as PlTLP1–4, were isolated identified from Picea likiangensis needles. Sequence analysis showed that PlTLP...

Thaumatin, an intensely sweet-tasting plant protein, elicits a sweet taste at a concentration of 50 nM. The crystal structure of a recombinant form of thaumatin I produced in the yeast Pichia pastoris has been determined to a resolution of 1.1 Å. The model was refined with anisotropic B parameters and riding H atoms. A comparison of the diffraction data and refinement statistics for recombinant...

In previous work, we showed that thaumatin, an intensely sweet protein, binds to certain formed elements in taste pores of Rhesus monkey foliate papillae, namely, microvilli and small vesicles shed from microvilli, in addition to amorphous secretions (Farbman et al., 1987). We suggested that the taste bud responds to a thaumatin stimulus by shedding the small vesicles containing fragments of mi...