Amino acid sequence analysis of bitter peptides from a soybean proglycinin subunit synthesized in Escherichia coli.
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.
Kim
M R
MR
Graduate School of Biotechnology, Korea University, Seoul, Korea.
Choi
S Y
SY
Kim
C S
CS
Kim
C W
CW
Utsumi
S
S
Lee
C H
CH
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics; D030262:Soybean Proteins; D013025:Glycine max / Q000737:chemistry*
D010940:Plant Proteins; D030262:Soybean Proteins; C405345:proglycinin A(1a)B(1b), soybean