| Autor: |
Prigent SV; Center for Protein Technology, TNO-WU, Wageningen, The Netherlands., Gruppen H, Visser AJ, Van Koningsveld GA, De Jong GA, Voragen AG |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of agricultural and food chemistry [J Agric Food Chem] 2003 Aug 13; Vol. 51 (17), pp. 5088-95. |
| DOI: |
10.1021/jf021229w |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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