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 |
| Publication status | Published - 1999 Dec 1 |
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Keywords
- Bitter peptide
- Proglycinin
- Soybean protein hydrolysate
ASJC Scopus subject areas
- Food Science
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology
- Chemistry (miscellaneous)
- Applied Microbiology and Biotechnology
- Bioengineering
Cite this
Amino acid sequence analysis of bitter peptides from a soybean proglycinin subunit synthesized in Escherichia coli. / Kim, Mi Ryung; Choi, Sang-Yun; Kim, Chan Shick; Kim, Chan Wha; Utsumi, Shigeru; Lee, Cherl Ho.
In: Bioscience, Biotechnology and Biochemistry, Vol. 63, No. 12, 01.12.1999, p. 2069-2074.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Amino acid sequence analysis of bitter peptides from a soybean proglycinin subunit synthesized in Escherichia coli
AU - Kim, Mi Ryung
AU - Choi, Sang-Yun
AU - Kim, Chan Shick
AU - Kim, Chan Wha
AU - Utsumi, Shigeru
AU - Lee, Cherl Ho
PY - 1999/12/1
Y1 - 1999/12/1
N2 - 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.
AB - 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.
KW - Bitter peptide
KW - Proglycinin
KW - Soybean protein hydrolysate
UR - http://www.scopus.com/inward/record.url?scp=0033255155&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033255155&partnerID=8YFLogxK
M3 - Article
C2 - 10664840
AN - SCOPUS:0033255155
VL - 63
SP - 2069
EP - 2074
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 12
ER -