FOOD SCIENCE ›› 2021, Vol. 42 ›› Issue (8): 67-73.doi: 10.7506/spkx1002-6630-20191018-183

• Food Chemistry • Previous Articles     Next Articles

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

JIA Na, LIN Shiwen, LIU Dan, LIU Dengyong   

  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 121013, China)
  • Online:2021-04-25 Published:2021-05-14

Abstract: 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.

Key words: rutin; myofibrillar protein; structure; gel properties; crosslinking

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