title: Hydrophobicity of bitter peptides from soy protein hydrolysates.
abstract: Soy peptides were characterized for flavor, chemical properties, and hydrophobicity to investigate their relationships with bitterness. Five peptide fractions ranging in average molecular mass from 580 to 11300 Da were fractionated by ultrafiltration from two commercial soy protein hydrolysates. The bitterness of fractionated peptides was related to molecular mass, with maximum bitterness observed at approximately 4000 Da for one hydrolysate and 2000 Da for the other. The bitterness increased as the peptide M(w) decreased to 3000 Da for the first hydrolysate and to 2000 Da for the second one and then decreased as the peptide M(w) decreased below 1000 Da. The peptide fraction with molecular mass of <1000 Da showed the lowest bitterness for both. The hydrophobicity data based on Q values do not support Ney's Q rule as a predictor of bitterness for soy peptides.
authors.affiliation: The Solae Company, St. Louis, Missouri 63188, and Department of Food Science, University of Missouri, Columbia, Missouri 65211, USA.
authors.forename: Myong J
authors.initials: MJ
authors.lastname: Cho
authors.forename: Nan
authors.initials: N
authors.lastname: Unklesbay
authors.forename: Fu-Hung
authors.initials: FH
authors.lastname: Hsieh
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Clarke
mesh_terms: D000596:Amino Acids / Q000032:analysis; D005591:Chemical Fractionation; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry*; D030262:Soybean Proteins / Q000737:chemistry*; D013649:Taste; D014462:Ultrafiltration
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D030262:Soybean Proteins