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Biosci Biotechnol Biochem. 1999 Dec;63(12):2069-74.

Amino acid sequence analysis of bitter peptides from a soybean proglycinin subunit synthesized in Escherichia coli.

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  • 1Graduate School of Biotechnology, Korea University, Seoul, Korea.


The cDNA encoding A1aB1b 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.

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