文献类型：期刊文献

英文题名：The structural rearrangement and depolymerisation induced by high-pressure homogenisation inhibit the thermal aggregation of myofibrillar protein

作者：Su, Chang[1];He, Zhifei[1,2,3];Wang, Zefu[4];Zhang, Dong[5];Li, Hongjun[1,2,3]

机构：[1]Southwest Univ, Coll Food Sci, 2 Tiansheng Rd, Chongqing 400715, Peoples R China;[2]Chongqing Engn Res Ctr Reg Food, 2 Tiansheng Rd, Chongqing 400715, Peoples R China;[3]Chongqing Key Lab Special Food Cobuilt Sichuan &, 2 Tiansheng Rd, Chongqing 400715, Peoples R China;[4]Guangdong Ocean Univ, Coll Food Sci & Technol, 1 Haida Rd, Zhanjiang 524088, Peoples R China;[5]Xihua Univ, Sch Food & Biol Engn, 999 Jinzhou Rd, Chengdu 610039, Peoples R China

年份：2022

卷号：57

期号：10

起止页码：6813

外文期刊名：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY

收录：SCI-EXPANDED(收录号：WOS:000849605800001)、、EI(收录号：20223712715471)、WOS

基金：The authors gratefully acknowledge financial support from China Agriculture Research System of MOF and MARA (Grant No. CARS-43-E-2), Chongqing Herbivorous Livestock Industry Technology System (Y201706) and Research project of Sichuan White Rabbit (2020JDZH0029).

语种：英文

外文关键词：Depolymerisation effect; high-pressure homogenisation; molecular rearrangement; myofibrillar protein; solubility; thermal aggregation

外文摘要：The effects of heating on the dissolution and aggregation of high-pressure homogenisation (HPH)-treated myofibrillar protein (MP) in low ionic strength medium were investigated in this study. Upon heating, HPH-treated MP (HTMP) had a greater solubility and lower turbidity than control MP (P < 0.05). The rheological measurement exhibited that the thermal aggregation ability of HTMP was hampered due to lower storage modulus (G ') and loss modulus (G ''), except near 50 degrees C. The increased G ' and G '' of HTMP at near 50 degrees C could be attributed to structural rearrangement induced by HPH. The analysis of proteomics indicated that HPH destroyed the cytoskeletal proteins in myofibrillar structure, made MP structure more swollen and flexible, promoted MP rearrangement and formation of oligomers with higher negative charge, which produced stronger steric hindrance and electrostatic repulsion between molecules, thus inhibiting thermally induced MP aggregation. The depolymerisation effect induced by HPH destroyed myosin head and tail portion, hampered the assembly of myosin into filaments and therefore suppressed the formation of strand-type aggregates under heating. The in vitro digestion suggested that the depolymerisation and rearrangement effect significantly improved MP digestibility (P < 0.05) regardless of whether the protein was heat treated or not.