食品科学2016，Vol.37Issue(13)：6-12,7.DOI:10.7506/spkx1002-6630-201613002
苦丁冬青苦丁茶咖啡酰奎尼酸类物质与α-淀粉酶的相互作用特性
Interaction Properties of Caffeoylquinic Acid Derivatives from Ilex kudingcha C. J. Tseng withα-Amylase
摘要
Abstract
The inhibitory effects of six caffeoylquinic acid (CQA) derivatives (3-CQA, 4-CQA, 5-CQA, 3,4-diCQA, 3,5-diCQA and 4,5-diCQA) againstα-amylase were studied comparatively by inhibitory activity assay. Furthermore, the potential interaction mechanisms between CQA derivative andα-amylase were investigated by fluorescence quenching and circular dichroism (CD) spectroscopy. The binding parameters were calculated according to modified Stern-Volmer equation, and the thermodynamic parameters were determined by the van’t Hoff equation. The results showed that all CQA derivatives exhibited inhibitory effects onα-amylase and the half inhibitory concentrations (IC50) were 1.54, 1.05, 1.28, 0.96, 0.33 and 0.64 mg/mL, respectively. CQA derivatives interacted withα-amylase, forming stable complexes and leading to fluorescence quenching. Thermodynamic analysis indicated that the interaction process was spontaneous, and hydrophobic force might be primarily responsible for the interaction. In addition, the CD spectra suggested that the binding of CQA derivatives to the enzyme induced the change of protein structure, thus destabilizing the enzyme and reducing its activity.关键词
α-淀粉酶/咖啡酰奎尼酸/荧光光谱/圆二色谱/相互作用Key words
α-amylase/caffeoylquinic acid/fluorescence spectroscopy/circular dichroism spectrum/interaction分类
轻工业引用本文复制引用
徐冬兰,王晴川,曾晓雄,孙怡..苦丁冬青苦丁茶咖啡酰奎尼酸类物质与α-淀粉酶的相互作用特性[J].食品科学,2016,37(13):6-12,7.基金项目
国家自然科学基金面上项目（31171666）；江苏高校优势学科建设工程资助项目 （）
