Effects of high pressure modification on conformation and gelation properties of myofibrillar protein

被引:331
|
作者
Zhang, Ziye [1 ,2 ,3 ]
Yang, Yuling [1 ]
Zhou, Peng [2 ,3 ]
Zhang, Xing [1 ]
Wang, Jingyu [1 ]
机构
[1] Nanjing Univ Finance & Econ, Key Lab Grains & Oils Qual Control & Proc, Collborat Innovat Ctr Modern Grain Circulat & Saf, Coll Food Sci & Engn, Nanjing 210023, Jiangsu, Peoples R China
[2] Jiangnan Univ, Sch Food Sci & Technol, State Key Lab Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China
[3] Collaborat Innovat Ctr Food Safety & Qual Control, Wuxi 214122, Jiangsu, Peoples R China
基金
中国国家自然科学基金;
关键词
Myofibrillar protein; High pressure; Conformation; Gelation property; SEM; DSC; RHEOLOGICAL CHARACTERISTICS; CHEMICAL FORCES; GEL; MEAT;
D O I
10.1016/j.foodchem.2016.09.040
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The effects of high pressure (HP) treatment (100-500 MPa) on conformation and gelation properties of myofibrillar protein (MP) were investigated. As pressure increased (0.1-500 MPa), alpha-helix and beta-sheet changed into random coil and beta-turn, proteins unfolded to expose interior hydrophobic and sulfhydryl groups, therefore surface hydrophobicity and formation of disulfide bonds were strengthened. At 200 MPa, protein solubility and gel hardness reached their maximum value, particle size had minimum value, and gel microstructure was dense and uniform. DSC data showed that actin and myosin completely denatured at 300 MPa and 400 MPa, respectively. Rheological modulus (G' and G '') of HP-treated MP decreased as pressure increased during thermal gelation. Moderate HP treatment (<= 200 MPa) strengthened gelation properties of MP, while stronger HP treatment (>= 300 MPa) weakened the gelation properties. 200 MPa was the optimum pressure level for modifying MP conformation to improve its gelation properties. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:678 / 686
页数:9
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