Effect of Fenton Oxidation Treatment on Structural and Functional Properties of Myofibrillar Proteins in Esox lucius Muslce

被引:0
作者
Deng X. [1 ]
Lei Y. [1 ]
Liu J. [1 ]
Lu S. [1 ]
Zhang J. [1 ]
机构
[1] School of Food Science and Technology, Shihezi University, Shihezi
来源
Shipin Kexue/Food Science | 2022年 / 43卷 / 06期
关键词
Esox lucius; Functional properties; Myofibrillar proteins; Protein oxidation; Structural properties;
D O I
10.7506/spkx1002-6630-20210331-387
中图分类号
学科分类号
摘要
The present study investigated the effects of different oxidation degrees (0, 1, 5, 10 and 20 mmol/L H2O2) induced by a Fenton oxidation system on the functional properties of myofibrillar proteins (MP) from Esox lucius muscle. Increasing oxidation degree caused an increase in carbonyl group content and turbidity and a significant decrease in protein solubility(P < 0.05). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed a greater degree of cross-linking and protein aggregation in oxidized MP. Fourier transform infrared spectroscopic (FTIR) analysis suggested that oxidation caused conformational changes in MP. The results of functional characterization indicated that moderate oxidation (1 and 5 mmol/L H2O2) substantially increased the foaming capacity of MP by 280% (P < 0.05) while having little effect on the emulsifying stability (which remained at above 90%). However, oxidation decreased the emulsifying properties of MP; the influence of moderate oxidation (1 and 5 mmol/L H2O2) was small, while excessive oxidation (> 10 mmol/L H2O2) led to a significant decrease in emulsifying capacity and emulsion stability. These results indicated that mild oxidation could improve the foaming capacity, and provide better functional properties of MP. © 2022, China Food Publishing Company. All right reserved.
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页码:27 / 33
页数:6
相关论文
共 51 条
[1]  
FORSMAN A, TIBBLIN P, BERGGREN H, Et al., Pike Esox lucius as an emerging model organism for studies in ecology and evolutionary biology: a review, Journal of Fish Biology, 87, 2, pp. 472-479, (2015)
[2]  
(2016)
[3]  
ESTEVEZ M., Oxidative damage to poultry: from farm to fork, Poultry Science, 94, 6, pp. 1368-1378, (2015)
[4]  
LUND M N, HEINONEN M, BARON C P, Et al., Protein oxidation in muscle foods: a review, Molecular Nutrition & Food Research, 55, 1, pp. 83-95, (2011)
[5]  
ZHANG W, XIAO S, AHN D U., Protein oxidation: basic principles and implications for meat quality, Critical Reviews in Food Science and Nutrition, 53, 11, pp. 1191-1201, (2013)
[6]  
ZHANG L, LI Q, JIA S, Et al., Effect of different stunning methods on antioxidant status, in vivo myofibrillar protein oxidation, and the susceptibility to oxidation of silver carp (Hypophthalmichthys molitrix)fillets during 72 h postmortem, Food Chemistry, 246, pp. 121-128, (2018)
[7]  
WANG L L, YU Q L, HAN L, Et al., Study on the effect of reactive oxygen species-mediated oxidative stress on the activation of mitochondrial apoptosis and the tenderness of yak meat, Food Chemistry, 244, pp. 394-402, (2018)
[8]  
ZOROV D B, JUHASZOVA M, SOLLOTT S J., Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release, Physiological Reviews, 94, 3, pp. 909-950, (2014)
[9]  
UTRERA M, ESTEVEZ M., Oxidation of myofibrillar proteins and impaired functionality: underlying mechanisms of the carbonylation pathway, Journal of Agricultural and Food Chemistry, 60, 32, pp. 8002-8011, (2012)
[10]  
XIONG Y L, BLANCHARD S P, OOIZUMI T, Et al., Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein, Journal of Food Science, 75, 2, pp. C215-C221, (2010)