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Effects of non-covalent interactions with 5-O-caffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins

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Author: Prigent, S.V.E. · Gruppen, H. · Visser, A.J.W.G. · Koningsveld, G.A. van · Jong, G.A.H. de · Voragen, A.G.J.
Source:Journal of Agricultural and Food Chemistry, 17, 51, 5088-5095
Identifier: 237222
doi: doi:10.1021/jf021229w
Keywords: Nutrition · Food technology · α-lactalbumin · BSA · Ionic strength · Lysozyme · PH · Phenolic compounds · Temperature · alpha lactalbumin · bovine serum albumin · chlorogenic acid · globular protein · lysozyme · acidity · alkalinity · article · covalent bond · enthalpy · food · high temperature · ionic strength · molecular interaction · protein denaturation · solubility · temperature dependence · temperature sensitivity · Chlorogenic Acid · Drug Interactions · Heat · Hydrogen-Ion Concentration · Lactalbumin · Muramidase · Osmolar Concentration · Protein Denaturation · Serum Albumin, Bovine · Solubility · Thermodynamics · Bovinae


The non-covalent interactions between the monomeric phenolic compound chlorogenic acid (5-CQA) and bovine serum albumin (BSA), lysozyme, and α-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 α-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.