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Isolation and Identification of Bitter Peptides of Tryptic Hydrolysate of Soybean 11S Glycinin by Reverse‐phase High‐performance Liquid Chromatography
Author(s) -
Kim I M.R.,
Kawamura Y.,
Lee C.H.
Publication year - 2003
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2003.tb07039.x
Subject(s) - hydrolysate , chemistry , chromatography , high performance liquid chromatography , bitter taste , peptide , gel permeation chromatography , taste , reversed phase chromatography , biochemistry , hydrolysis , organic chemistry , polymer
ABSTRACT: The 21 peptides purified from the bitter fraction of tryptic hydrolysates of soybean 11S glycinin by using gel‐permeation high‐performance liquid chromatography (HPLC) and a series of 3 C 18 reverse phase (RP)‐HPLC were in the molecular weight range of 200‐1400 Da and showed mostly the hydrophobicity of less than 1400 cal/mol. Although the primary structures of the bitter peptides from 11S glycinin were not exactly the same as those of the proglycinin, many bitter peptides were basic mimics of the common structure, indicating the significance of the primary structure of a peptide playing a role in the bitter taste perception.