文献类型：期刊文献

英文题名：Effect of protein structure changes during different power ultrasound thawing on emulsification properties of common carp (Cyprinus carpio) myofibrillar protein

作者：Sun, Qinxiu[1,2]; Kong, Baohua[3]; Zheng, Ouyang[1]; Liu, Shucheng[1]; Dong, Xiuping[2]

机构：[1] College of Food Science and Technology, Guangdong Ocean University, Guangdong, Zhanjiang, 524088, China; [2] School of Food Science and Technology, Dalian Polytechnic University, Dalian, 116034, China; [3] College of Food Science, Northeast Agricultural University, Heilongjiang, Harbin, 150030, China

年份：2023

卷号：101

外文期刊名：Ultrasonics Sonochemistry

收录：EI(收录号：20235115231607)、Scopus(收录号：2-s2.0-85179628290)

语种：英文

外文关键词：Biomarkers - Emulsification - Proteins - Structural properties - Thawing - Thermodynamic stability

外文摘要：The impact of ultrasound thawing (UT) at different power (0 W, 100 W/0.132 W·cm?2, 300 W/1.077 W·cm?2, and 500 W/1.997 W·cm?2, namely WT, UT-100, UT-300, and UT-500) on protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein were investigated in the present study. The result showed that the reactive sulfhydryl content, total sulfhydryl content, protein solubility, and absolute potential of UT-300 samples were obviously higher than those of other thawed samples, while the turbidity of UT-300 samples was lower (P 2+-ATPase activity and thermal stability of UT-300 samples were much higher than those of other thawed samples (P max of UT-300 samples and UT-100 samples were lower than that of other thawed samples, which indicated that UT-300 could effectively inhibit the alteration of protein secondary structure and tertiary structure during thawing. The emulsifying activity of UT-300 samples was significantly higher than that of WT samples, and the droplet diameter of UT-300 samples was also lower than that of WT samples (P ? 2023 The Author(s)