Interaction of Protein Isolate with Anthocyanin Extracted from Black Soybean and Its Effect on the Anthocyanin Stability

被引:30
|
作者
Wang, Chen [1 ,2 ]
Xie, Yanli [1 ,2 ]
机构
[1] Henan Univ Technol, Sch Food Sci & Technol, Zhengzhou 450001, Henan, Peoples R China
[2] Henan Key Lab Cereal & Oil Food Safety Inspect &, Zhengzhou 450001, Henan, Peoples R China
基金
国家重点研发计划;
关键词
cyanidin; 3-O-glucoside; fluorescence quenching; interactions; neutral conditions; secondary structure; thermal stability; HUMAN SERUM-ALBUMIN; WHEY-PROTEIN; FUNCTIONAL-PROPERTIES; ENHANCED STABILITY; THERMAL-STABILITY; BINDING; COLOR; COPIGMENTATION; DEGRADATION; ACID;
D O I
10.1111/1750-3841.14816
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The interactions between black soybean protein isolate (B-SPI) and cyanidin 3-O-glucoside (C3G), anthocyanin extracted from black soybean coat was investigated under neutral conditions. The fluorescence spectra showed that C3G had fluorescence quenching effects on B-SPI. Thermodynamic parameters showed that increment G < 0, which demonstrated that the binding was a spontaneous reaction. Since Delta H > 0 and Delta S > 0, the interactions between C3G and B-SPI was mainly hydrophobic interactions. Fourier infrared spectroscopy results suggested that the contents of alpha-helix and beta-sheet structure showed an increasing trend, whereas the beta-angle content displayed a decreasing trend. The degradation of C3G followed first-order kinetics at 85 degrees C and 100 degrees C. After the interactions with B-SPI, the degradation rate constant was decreased and the half-life of C3G was prolonged from 70.25 +/- 0.90 min to 175.64 +/- 38.04 min at 85 degrees C, from 62.68 +/- 1.1 min to 72.51 +/- 2.5 min at 100 degrees C (p < 0.05). The results indicated that the interactions of B-SPI and C3G improved the thermal stability of C3G under heating conditions.
引用
收藏
页码:3140 / 3146
页数:7
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