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 |
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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