Effects of non-covalent interactions with 5-O-caffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins
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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DOI：
10.1021/jf021229w
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发表时间：
2003-08-13
影响因子：
6.1
通讯作者：
Voragen, AGJ
中科院分区：
文献类型：
--
作者：
Prigent, SVE;Gruppen, H;Voragen, AGJ
研究了单酚类化合物绿原酸（5-CQA）与牛血清白蛋白（BSA）、溶菌酶和乳清蛋白之间的非共价相互作用，并考察了它们对蛋白质性质的影响。5-CQA对这三种蛋白的亲和力都很低，这些相互作用似乎表现出负的协同性。随着温度的升高，5-辅酶a - bsa结合降低，而pH （pH 3.0比pH 7.0）和离子强度对5-辅酶a - bsa结合无明显影响。高5-CQA/蛋白摩尔比时，牛血清白蛋白的变性焓和变性温度均升高；然而，共价键是在高温下形成的。5-CQA的存在对牛血清白蛋白和乳清蛋白的溶解度没有影响，但由于共价相互作用，它在碱性pH下降低了溶菌酶的溶解度。这些结果表明，与5-CQA的非共价相互作用对食品系统中球状蛋白的功能特性没有明显的影响。
The non-covalent interactions between the monomeric phenolic compound chlorogenic acid (5-CQA) and bovine serum albumin (BSA), lysozyme, and a-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-COA-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 a-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.