食品抗氧化剂叔丁基对苯二酚与溶菌酶结合特性的荧光光谱学研究

Fluorescence Spectroscopy Studies on Binding Properties of Food Antioxidant Tert-butylhydroquinone and Lysozyme

叔丁基对苯二酚是一种被广泛应用的脂溶性酚类食品抗氧化剂,为揭示食品抗氧化剂叔丁基对苯二酚与溶菌酶的相互作用机理,利用荧光猝灭、同步荧光、三维荧光与荧光寿命的测定,从结合机理、亲和能力及结构改变等方面分析了叔丁基对苯二酚与溶菌酶的结合特性.结果表明:叔丁基对苯二酚能与溶菌酶形成不发光的基态复合物,常温下的结合常数约为3×104L/mol;该结合过程属自发行为,且氢键和范德华力在此过程中起主导作用;叔丁基对苯二酚的嵌插促使复合物的形成,并改变了溶菌酶的原有氨基酸残基微环境,但蛋白整体构象保持完整.

Tert-butylhydroquinone is used worldwide as a phenolic food antioxidant. The main aim of this study is to reveal the interaction between tert-butylhydroquinone and lysozyme. The binding properties are explained from the aspects of binding mechanism, affinity ability and structural changes via fluorescence ti-tration, synchronous fluorescence, three-dimensional fluorescence, and fluorescence lifetime. The results show that tert-butylhydroquinone combined with lysozyme can form a nonluminous ground state complex and the binding constant at normal temperature is about 3 x 10^4 L/tool. The binding process is spontaneous ma-inly driven by hydrogen bonds and Van Der Waals forces. The integration of tertbutylhydroquinone and the lysozyme can promote the formation of the complex and the original mieroenvironment of the amino acid res-idue changes but the whole eonformation of the albumen remains intact.