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• W2149148919 endingPage "5095" @default.
• W2149148919 startingPage "5088" @default.
• W2149148919 abstract "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." @default.
• W2149148919 created "2016-06-24" @default.
• W2149148919 creator A5027089451 @default.
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• W2149148919 date "2003-07-12" @default.
• W2149148919 modified "2023-10-10" @default.
• W2149148919 title "Effects of Non-covalent Interactions with 5-<i>O</i>-Caffeoylquinic Acid (Chlorogenic Acid) on the Heat Denaturation and Solubility of Globular Proteins" @default.
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• W2149148919 doi "https://doi.org/10.1021/jf021229w" @default.
• W2149148919 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12903974" @default.
• W2149148919 hasPublicationYear "2003" @default.
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