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Isolation of Low‐Molecular‐Weight Taste Peptides from Vacherin Mont ?Or Cheese
Author(s) -
MOJARROGUERRA SANDRA H.,
AMADÒ RENATO,
ARRIGONI EVI,
SOLMS JUERG
Publication year - 1991
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.1365-2621.1991.tb14611.x
Subject(s) - chemistry , chromatography , ultrafiltration (renal) , peptide , sephadex , glycine , high performance liquid chromatography , amino acid , taste , biochemistry , enzyme
Vacherin cheese samples weie extracted with water and the extracts fractionated by ultrafiltration excluding compounds with a molecular weight less than 1,000. Extract aliquots were fractionated by ligand exchange chromatography on a Sephadex derivative containing N‐(2‐pyridylmethyl)glycine‐groups in Cu 2+ form, permitting a specific group separation of peptides. Five peptide sub‐groups were then chromato‐graphed on Aminex A6 and Durrum DC 4 resin. Nine fractions from these separations were characterized by manual gas‐phase isofhiocy‐anate degradation and HPLC of the amino acid derivatives. Seven peptides could be identified: H‐Leu‐Pro‐OH, H‐Val‐Pro‐OH, H‐Phe‐Pro‐OH, H‐Lys‐Pro‐OH, H‐Gly‐Pro‐Val‐Arg‐OH, H‐Tyr‐Pro‐OH, and H‐Arg‐Pro‐OH. A partial elucidation of the structure was possible for peptides containing Asp/Pro/Val/Leu, Glu/Leu, and Ala/Pro.