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 language | English |
|---|---|
| Pages (from-to) | 2069-2074 |
| Number of pages | 6 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 63 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 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
Fingerprint Dive into the research topics of 'Amino Acid Sequence Analysis of Bitter Peptides from a Soybean Proglycinin Subunit Synthesized in Escherichi'. Together they form a unique fingerprint.
Cite this
Kim, M. R., Choi, S. Y., Kim, C. S., Kim, C. W., Utsumi, S., & Lee, C. H. (1999). Amino Acid Sequence Analysis of Bitter Peptides from a Soybean Proglycinin Subunit Synthesized in Escherichi. Bioscience, Biotechnology and Biochemistry, 63(12), 2069-2074. https://doi.org/10.1271/bbb.63.2069