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The binding of the flavour of lactones by soya protein, amino acids and casein
Author(s) -
Gkionakis George A.,
David Anthony Taylor Keith,
Ahmad John,
Heliopoulos George
Publication year - 2007
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2006.01184.x
Subject(s) - chemistry , hydrogen bond , van der waals force , ligand (biochemistry) , amino acid , casein , chromatography , hydrophobic effect , gas chromatography , stereochemistry , organic chemistry , molecule , biochemistry , receptor
Summary The binding of certain lactones to soya protein isolate, amino acids and casein in different concentrations was investigated using capillary column gas chromatography. The analysis of lactones was conducted by solid phase microextraction and by the standard method of headspace analysis. The percentage of binding of lactones γ ‐9, γ ‐10, δ ‐10 and δ ‐11 on the soya protein is almost the same. According to the Klotz equation, the bound ligand concentration was calculated as the number of moles of ligand bound per mole of protein. γ ‐lactones are bound less than δ ‐lactones and that the competitive binding ability of lactones δ ‐11 and γ ‐10 is similar. δ ‐11 has a greater binding capacity with each of the amino acids used and with casein than γ ‐10 because of its greater ability to form hydrophobic binding than γ ‐10. The techniques of gas chromatography/mass spectrometry and infrared spectroscopy confirmed that the binding of the ligand on the protein substrate was attributed to secondary bonds, such as hydrogen bonds, hydrophobic bonds and van der Waals forces.