Class of low calorie protein sweeteners

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues

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435 691, 4352402, 4353201, 530300, 530350, 530370, 5303871, 530402, 530323, 530324, 536 221, 536 231, 536 234, 536 236, 536 242, C07K 100, C07K 200, C12P 2106, A61K 3514

Patent

active

054789230

ABSTRACT:
Single-chain analogs of the naturally occurring two-chain peptide monellin retain the sweetening properties of the natural protein and are stable under conditions which would otherwise destabilize the native peptide. A covalent linkage joins peptides corresponding to portions of the A and B chains of the naturally occurring protein.

REFERENCES:
patent: 3998798 (1976-12-01), Cagan et al.
De Vos et al., Three-dimensional structure of thaumatin I, an intensely sweet protein; Proc. Natl. Acad. Sci. USA (1985) 82:1406-1409.
Ogata et al., Crystal structure of the intensely sweet protein monellin; Nature (1987) 328:739-742.
Morris et al., Characterization of monellin, a protein that tastes sweet; J. Biol. Chem. (1973) 248:534-539.
Cagan R. H., Chemostimulatory protein: A new type of taste stimulus; Science (1973) 181:32-25.
Bohak et al., The structure of monellin and its relation to the sweetness of the protein; Biochim. Biophys. Acta. (1976) 427:153-170.
Hudson et al., Mass spectrometric sequencing of proteins. The structure of subuit I of monellin; Biochem. Biophys. Res. Comm. (1976) 71:212-220.
Van der Wel et al., Characterization of the sweet-tasting protein from dioscoreophyllum cumminsi (Stapf) diels; FEBS Lett (1973) 29:181-183.
Frank et al., The complete amino acid sequences of both subunits of the sweet protein monellin; Z. Physiol. Chem. (1976) 357:585-592.
Morris et al., Purification of monellin, the sweet principle of dioscoreophyllum cumminsii; Biochim. Biophys. Acta. (1972) 261:114-122.

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