文献类型：期刊文献

英文题名：Study of Ca2+-ATPase Activity and Solubility in the Whole Kuruma Prawn (Marsupenaeus japonicus) Meat During Heating: Based on the Kinetics Analysis of Myofibril Protein Thermal Denaturation

作者：Mao, Weijie[1]; Li, Xiaolong[1]; Fukuoka, Mika[2]; Liu, Shucheng[1]; Ji, Hongwu[1]; Sakai, Noboru[2]

机构：[1] Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Key Laboratory of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524088, China; [2] Department of Food Science and Technology, Tokyo University of Marine Science and Technology, Konnan 4-chome, Minato, Tokyo, 108-8477, Japan

年份：2016

卷号：9

期号：9

起止页码：1511

外文期刊名：Food and Bioprocess Technology

收录：EI(收录号：20162002372778)、Scopus(收录号：2-s2.0-84966393310)

语种：英文

外文关键词：Calorimeters - Kinetics - Denaturation - Proteins - Hydrophobicity - Chemical analysis - Heating - Shellfish - Solubility - Activation energy - Hydrogen bonds

外文摘要：Protein denaturation is considered to be the main cause of physicochemical changes in prawns during heating. However, no studies have been analyzed the kinetics of protein denaturation and the relationship between the degree of denaturation and chemical changes. Therefore, we investigated the changes in Ca2+-ATPase activity, protein solubility, and total sulfhydryl content of whole prawn meat during heating by determining the thermal denaturation kinetics of the proteins. Activation energies (Ea) for the denaturation of myosin (183.2?kJ/mol) and actin (178.8?kJ/mol) were obtained by non-isothermal differential scanning calorimetry analysis. Using the kinetic parameters, the distribution of protein denaturation was predicted in whole prawns under arbitrary heating conditions. The results revealed an uneven distribution of the protein denaturation in prawns that was dependent on the heating conditions. Ca2+-ATPase activity decreased with increasing heating times at 51 or 85?°C and was strongly related to the average degree of protein denaturation. The results of protein solubility analysis suggested that hydrogen bonds, hydrophobic interactions, and ionic bonds changed with protein denaturation. The number of ionic bonds was reduced, while hydrogen content was enhanced at both temperatures. Hydrophobic interactions increased gradually at 51?°C (p 0.05). Our results indicate that the extent of protein solubility is significantly correlated with the average degree of protein denaturation during the heating process. ? 2016, Springer Science+Business Media New York.