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Changes in the myosin secondary structure and shrimp surimi gel strength induced by dense phase carbon dioxide  ( SCI-EXPANDED收录 EI收录)   被引量:72

文献类型:期刊文献

英文题名:Changes in the myosin secondary structure and shrimp surimi gel strength induced by dense phase carbon dioxide

作者:Guo, Minghui[1];Liu, Shucheng[1];Ismail, Marliya[2];Farid, Mohammed M.[2];Ji, Hongwu[1];Mao, Weijie[1];Gao, Jing[1];Li, Chengyong[1]

机构:[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Seafood Engn Technol Res Ctr,Guang, Key Lab Adv Proc Aquat Prod Guangdong Higher Educ, Zhanjiang, Peoples R China;[2]Univ Auckland, Dept Chem & Mat Engn, Auckland, New Zealand

年份:2017

卷号:227

起止页码:219

外文期刊名:FOOD CHEMISTRY

收录:SCI-EXPANDED(收录号:WOS:000396957100029)、、EI(收录号:20170503297636)、Scopus(收录号:2-s2.0-85010682879)、WOS

基金:This work was supported by the National Natural Science Foundation of China [31371801]; Science and Technology Planning Project of Guangdong [2015A020209158]; and Modern Agroindustry Technology Research System of China [CARS-47].

语种:英文

外文关键词:Dense phase carbon dioxide; Secondary structure; Gel strength; Myosin; Shrimp surimi

外文摘要:Dense phase carbon dioxide (DPCD) could induce protein conformation changes. Myosin and shrimp surimi from Litopenaeus vannamei were treated with DPCD at 5-25 MPa and 40-60 degrees C for 20 min. Myosin secondary structure was investigated by circular dichroism and shrimp surimi gel strength was determined using textural analysis to develop correlations between them. DPCD had a greater effect on secondary structure and gel strength than heating. With increasing pressure and temperature, the alpha-helix content of DPCD-treated myosin decreased, while the beta-sheet, beta-turn and random coil contents increased, and the shrimp surimi gel strength increased. The a-helix content was negatively correlated with gel strength, while the beta-sheet, beta-turn and random coil contents were positively correlated with gel strength. Therefore, when DPCD induced myosin to form a gel, the a-helix of myosin was unfolded and gradually converted to a beta-sheet. Such transformations led to protein-protein interactions and cross-linking, which formed a three-dimensional network to enhance the gel strength. (C) 2017 Elsevier Ltd. All rights reserved.

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