Effects of non-covalent interactions with 5-O-caffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins
article
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.
Topics
Food technologyα-lactalbuminBSAIonic strengthLysozymePHPhenolic compoundsTemperatureAlpha lactalbuminBovine serum albuminChlorogenic acidGlobular proteinLysozymeAcidityAlkalinityCovalent bondEnthalpyFoodHigh temperatureIonic strengthMolecular interactionProtein denaturationSolubilityTemperature dependenceTemperature sensitivityChlorogenic AcidDrug InteractionsHeatHydrogen-Ion ConcentrationLactalbuminMuramidaseOsmolar ConcentrationProtein DenaturationSerum Albumin, BovineSolubilityThermodynamicsBovinae
TNO Identifier
237222
ISSN
00218561
Source
Journal of Agricultural and Food Chemistry, 51(17), pp. 5088-5095.
Pages
5088-5095
Files
To receive the publication files, please send an e-mail request to TNO Repository.