This study was partially supported by the grant of Korea Science and Engineering Foundation (No. KOSEF96-0402-05-01-3).
Isolation and Identification of Bitter Peptides of Tryptic Hydrolysate of Soybean 11S Glycinin by Reverse-phase High-performance Liquid Chromatography
Article first published online: 20 JUL 2006
Journal of Food Science
Volume 68, Issue 8, pages 2416–2422, October 2003
How to Cite
Kim, I. M.-R., Kawamura, Y. and Lee, C.-H. (2003), Isolation and Identification of Bitter Peptides of Tryptic Hydrolysate of Soybean 11S Glycinin by Reverse-phase High-performance Liquid Chromatography. Journal of Food Science, 68: 2416–2422. doi: 10.1111/j.1365-2621.2003.tb07039.x
- Issue published online: 20 JUL 2006
- Article first published online: 20 JUL 2006
- MS 20030158 Submitted 5/26/03, Revised 5/9/03, Accepted 7/21/03.
- soybean 11S glycinin;
- bitter peptides;
- amino acid sequence;
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 C18 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.