Amino Acid Sequence Analysis of Bitter Peptides from a Soybean Proglycinin Subunit Synthesized in Escherichia coli

概要

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The cDNA encoding A_<1a>B_<1b> proglycinin was expressed in E.coli, for the efficient isolation of a single peptide responsible for the bitterness. The 55-kD proglycinin was highly purified, hydrolyzed, and further purified through a series of chromatographic steps to yield fractions with the major bitter peptides. The most bitter-tasting fractions contained peptides with average molecular weights lower than 1,700 Da. An analysis of the amino acid sequences indicated that many small bitter peptides (<1,000 Da) are composed of uncharged polar amino acids as well as hydrophobic amino acids, with a charged residue often being present at either end. This suggests the involvement of a certain structural requirement in taste perception.
社団法人日本農芸化学会の論文
1999-12-23