Improvement Effects of Structural Changes of Pork Myofibrillar Protein Induced by Rutin on Its Gel Properties

被引:1
作者
Jia N. [1 ]
Lin S. [1 ]
Liu D. [1 ]
Liu D. [1 ]
机构
[1] National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, Food Safety Key Lab of Liaoning Province, College of Food Science and Technology, Bohai University, Jinzhou
来源
Shipin Kexue/Food Science | 2021年 / 42卷 / 08期
关键词
Crosslinking; Gel properties; Myofibrillar protein; Rutin; Structure;
D O I
10.7506/spkx1002-6630-20191018-183
中图分类号
学科分类号
摘要
Different concentrations of rutin (0, 10, 50, 100 and 150 μmol/g protein) was added to Fenton oxidation system containing pork myofibrillar protein (40 mg/mL protein, 10 μmol/L FeCl3, 100 μmol/L VC and 1 mmol/L H2O2). To study the effects of rutin on the structure and gel properties of myofibrillar protein, we determined the sulfhydryl content, surface hydrophobicity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) pattern, solubility, gel strength, water-holding capacity and rheological properties of the protein. The results showed that the addition of rutin significantly decreased the sulfhydryl content of myofibrillar protein (P < 0.05), and first decreased and then increased the surface hydrophobicity. Rutin addition reduced the intensity of myosin heavy chain (MHC). The intensity of actin band was decreased at higher concentrations of rutin (100 and 150 μmol/g). Most of the MHC and actin bands were restored after adding β-mercaptoethanol. The solubility was decreased with increasing rutin concentration, and the gel strength and water-holding capacity were increased significantly (P < 0.05). Similarly, the storage modulus (G') in the final stage of gel formation was increased. Therefore, rutin can improve the gel properties of myofibrillar protein by covalent crosslinking with it or moderately increasing its surface hydrophobicity. © 2021, China Food Publishing Company. All right reserved.
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页码:67 / 73
页数:6
相关论文
共 29 条
[1]  
LORENZO J M, VARGAS F C, STROZZI I, Et al., Influence of pitanga leaf extracts on lipid and protein oxidation of pork burger during shelf-life, Food Research International, 114, pp. 47-54, (2018)
[2]  
FENG X C, CHEN L, LEI N, Et al., Emulsifying properties of oxidatively stressed myofibrillar protein emulsion gels prepared with(-)-epigallocatechin-3-gallate and NaCl, Journal of Agricultural and Food Chemistry, 65, 13, pp. 2816-2826, (2017)
[3]  
JONGBERG S, SKOV S H, TORNGREN M A, Et al., Effect of white grape extract and modified atmosphere packaging on lipid and protein oxidation in chill stored beef patties, Food Chemistry, 128, 2, pp. 276-283, (2011)
[4]  
TURGUT S S, ISIKCI F, SOYER A., Antioxidant activity of pomegranate peel extract on lipid and protein oxidation in beef meatballs during frozen storage, Meat Science, 129, pp. 111-119, (2017)
[5]  
OZDAL T, CAPANOGLU E, ALTAY F., A review on protein-phenolic interactions and associated changes, Food Research International, 51, 2, pp. 954-970, (2013)
[6]  
JONGBERG S, TERKELSEN L S, MIKLOS R, Et al., Green tea extract impairs meat emulsion properties by disturbing protein disulfide cross-linking, Meat Science, 100, pp. 2-9, (2015)
[7]  
JIA N, WANG L T, SHAO J H, Et al., Changes in the structural and gel properties of pork myofibrillar protein induced by catechin modification, Meat Science, 127, pp. 45-50, (2017)
[8]  
CAO Y G, XIONG Y L., Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein, Food Chemistry, 180, pp. 235-243, (2015)
[9]  
TANG C B, ZHANG W G, ZOU Y F, Et al., Influence of RosA-protein adducts formation on myofibrillar protein gelation properties under oxidative stress, Food Hydrocolloids, 67, pp. 197-205, (2017)
[10]  
7