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Food Chem. 2017 Feb 15;217:678-686. doi: 10.1016/j.foodchem.2016.09.040. Epub 2016 Sep 7.

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

Author information

1
College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety/Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, PR China; State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, PR China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, Jiangsu Province 214122, PR China. Electronic address: ziyezhangnj@gmail.com.
2
College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety/Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, PR China. Electronic address: yulingy@163.com.
3
State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu Province 214122, PR China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi, Jiangsu Province 214122, PR China.
4
College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety/Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, PR China.

Abstract

The effects of high pressure (HP) treatment (100-500MPa) on conformation and gelation properties of myofibrillar protein (MP) were investigated. As pressure increased (0.1-500MPa), α-helix and β-sheet changed into random coil and β-turn, proteins unfolded to expose interior hydrophobic and sulfhydryl groups, therefore surface hydrophobicity and formation of disulfide bonds were strengthened. At 200MPa, 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 300MPa and 400MPa, respectively. Rheological modulus (G' and G″) of HP-treated MP decreased as pressure increased during thermal gelation. Moderate HP treatment (≦200MPa) strengthened gelation properties of MP, while stronger HP treatment (⩾300MPa) weakened the gelation properties. 200MPa was the optimum pressure level for modifying MP conformation to improve its gelation properties.

KEYWORDS:

Conformation; DSC; Gelation property; High pressure; Myofibrillar protein; SEM

PMID:
27664686
DOI:
10.1016/j.foodchem.2016.09.040
[Indexed for MEDLINE]

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