文献类型：期刊文献

英文题名：Cryoprotective effect of magnetic field-assisted freezing in combination with curdlan on myofibrillar protein of Litopenaeus vannamei: Oxidative aggregation, protein structure and thermal stability

作者：Lu, Minxin[1];Zhang, Chang[1];Ma, Linyin[1];Liu, Shucheng[1];Teng, Hui[1];Chen, Lei[1,2]

机构：[1]Guangdong Ocean Univ, Guangdong Higher Educ Inst, Coll Food Sci & Technol, Key Lab Adv Proc Aquat Prod,Guangdong Prov Engn Te, Zhanjiang 524088, Peoples R China;[2]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518108, Peoples R China

年份：2025

卷号：160

外文期刊名：FOOD HYDROCOLLOIDS

收录：SCI-EXPANDED(收录号：WOS:001347172100001)、、EI(收录号：20244417279883)、Scopus(收录号：2-s2.0-85207653215)、WOS

基金：This work is supported by the Guangdong Basic and Applied Basic Research Foundation (2024B1515020110) , Key Field Project Supported by Educational Commission of Guangdong Province (Biological Medicine and Health) (2022 ZDZX2028) , College student innovation team of Guangdong Ocean University (CXTD2024003) .

语种：英文

外文关键词：Magnetic field assisted freezing; Curdlan; Myofibrillar protein; Oxidative denaturation

外文摘要：To counteract the negative effects of conventional freezing methods on frozen surimi products, the present study investigated the effects of magnetic field (MF) freezing in combination with different amounts of curdlan (CUR) on oxidative denaturation, structural alterations, and thermal stability of myofibrillar protein (MP) in shrimp surimi. The results indicated that the intervention of magnetic fields alone improved the quality of frozen muscle proteins. Under the dual intervention of magnetic field-assisted freezing and CUR, small ice crystals formed with MF6 treatment resulted in significantly lower solubility, turbidity, and mean particle size than the control group (p < 0.05). Moreover, the oxidation of MP was also significantly slowed down by inhibiting the formation of hydrophobic groups and carbonyl groups, maintaining a high content of sulfhydryl groups. MF6 also exhibited a high Ca2+-ATPase activity. The alpha-helix content, the increase in fluorescence intensity under this condition also tend to make the secondary and tertiary structures of myofibrillar protein more stable. Meanwhile, electrophoretic profiles and CLSM showed that this condition maintains the integrity of the MP. In addition, the MF6 samples also had high protein thermal stability. However, excess CUR reduces the excellence of MP cryoprotection. As a result, MF6 has better protection and improvement effects on protein function, structure and thermal stability, and CUR was also found to have the potential for cryoprotectant development.