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Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin.
The taste-modifying protein, miraculin, has the unusual property of modifying sour taste into sweet taste and high homology was found between the amino acid sequences of miraculin and soybean trypsin inhibitor. Expand
Purification and complete amino acid sequence of a new type of sweet protein taste-modifying activity, curculin.
The results suggest that native curculin is a dimer of a 12,000-Da polypeptide, which elicits a sweet taste and sour substances induce a stronger sense of sweetness. Expand
Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II.
High similarity was found between the amino acid sequences of mabinlin II and 2S seed storage proteins, especially 2S albumin AT2S3 in Arabidopsis thaliana (mouse-ear cress). Expand
Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit.
The taste-modifying protein, miraculin, has the unusual property of modifying a sour taste into a sweet taste and is extracted with 0.5 M NaCl solution, indicating that it is highly pure. Expand
Characteristics of antisweet substances, sweet proteins, and sweetness-inducing proteins.
  • Y. Kurihara
  • Chemistry, Medicine
  • Critical reviews in food science and nutrition
  • 1992
Several gymnemic acid homologues and gurmarin were purified from the leaves of Gymnema sylvestre and their structures were determined, expected to be used as low-calorie sweeteners. Expand
Determination of disulfide array and subunit structure of taste-modifying protein, miraculin.
It was concluded that native miraculin in pure form is a tetramer of the 25 kDa-peptide and native miracleulin in crude state or denatured, non-reduced miraculin onyx-containing peptides isolated by HPLC had the taste-modifying activity. Expand
Recombinant curculin heterodimer exhibits taste‐modifying and sweet‐tasting activities
It was revealed that sweet‐tasting and taste‐modifying activities were exhibited solely by the heterodimer of curculin1 andCurculin2. Expand
Cloning and sequencing of a cDNA encoding a taste-modifying protein, miraculin.
A cDNA clone encoding a taste-modifying protein, miraculin (MIR), was isolated and sequenced and showed that the mRNA encoding MIR was already expressed in fruits of Richadella dulcifica at 3 weeks after pollination and was present specifically in the pulp. Expand
Activity and stability of a new sweet protein with taste-modifying action, curculin.
The sweetness induced by deionized water was completely suppressed by the presence of 1 mM CaCl2 or MgCl2, while that induced by an acid was not suppressed byThe presence of divalent cations. Expand
Studies on taste modifiers. II. Purification and structure determination of gymnemic acids, antisweet active principle from Gymnema sylvestre leaves
Abstract Two major active components of gymnemic acids were isolated in pure state. Their chemical structures were established as D-glucuronide of 3β,16β,21β,22α,23,28-hexahydroxyolean-12-ene whichExpand