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

Mi Ryung Kim, Sang Yun Choi, Chan Shick Kim, Chan Wha Kim, Shigeru Utsumi, Cherl Ho Lee

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2069-2074
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Volume63
Issue number12
DOIs
Publication statusPublished - 1999 Jan 1

Keywords

  • Bitter peptide
  • Proglycinin
  • Soybean protein hydrolysate

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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