Effects of non-covalent interactions with 5-O-caffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins.
The non-covalent interactions between the monomeric phenolic compound chlorogenic acid (5-CQA) and bovine serum albumin (BSA), lysozyme, and alpha-lactalbumin were characterized, and their effect on protein properties was examined. 5-CQA had a low affinity for all three proteins, and these interactions seemed to show a negative cooperativity. 5-CQA-BSA binding decreased with increasing temperature, whereas pH (pH 3.0 compared to pH 7.0) and ionic strength had no pronounced effect. At high 5-CQA/protein molar ratios, both the denaturation enthalpy and temperature of BSA increased; however, covalent bonds were created at high temperatures. The presence of 5-CQA had no effect on the solubility of BSA and alpha-lactalbumin as a function of pH, whereas it decreased lysozyme solubility at alkaline pH due to covalent interactions. These results indicate that the non-covalent interactions with 5-CQA do not have pronounced effects on the functional properties of globular proteins in food systems.
Prigent
Stéphanie V E
SV
Center for Protein Technology, TNO-WU, Wageningen, The Netherlands.
Gruppen
Harry
H
Visser
Antonie J W G
AJ
Van Koningsveld
Gerrit A
GA
De Jong
Govardus A H
GA
Voragen
Alfons G J
AG
D002726:Chlorogenic Acid / Q000737:chemistry*; D004347:Drug Interactions; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007768:Lactalbumin / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D009994:Osmolar Concentration; D011489:Protein Denaturation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012995:Solubility; D013816:Thermodynamics
D012710:Serum Albumin, Bovine; D002726:Chlorogenic Acid; D007768:Lactalbumin; D009113:Muramidase