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CHARACTERIZATION OF THE CHLOROGENIC ACID BINDING FRACTION IN LEAF PROTEIN CONCENTRATION
Author(s) -
LAHIRY N. L.,
SATTERLEE L. D.,
HSU H. W.,
WALLACE G. W.
Publication year - 1977
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.1365-2621.1977.tb01223.x
Subject(s) - chlorogenic acid , chemistry , in vitro , chromatography , fraction (chemistry) , biochemistry , trypsin , phosphate buffered saline , ingredient , food science , enzyme
Leaf protein concentrate (LPC) haa been shown to have the phenolic acid, chlorogenic acid, bound to its protein molecules. Bound chlorogenie acid creates off color problems in foods containing LPC as an ingredient and also possibly lowers the digestibility of LPC by inhibiting the rate of trypsin attack on the protein. A buffer, containing 2.5% NaCl‐1 mM mercaptoethanol‐40 mM phosphate, effectively removed 69% of the chiorogenic acid from LPC. LPC, with the majority of its chlorogenic acid removed, had an enhanced in vitro protein digestibility and an amino acid pattern very similar to that of the original LPC. A series of small molecular weight proteins were found to be the chlorogenie acid binding fraction in LPC.