Improvement of myofibrillar protein gel strength of Scomberomorus niphonius by riboflavin under UVA irradiation
Baoyu He
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorYixin Shi
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorMeiran Jin
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorYuan Pu
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorXiuping Dong
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorChenxu Yu
Department of Agricultural and Biosystems Engineering, Iowa State University, Ames, Iowa
Search for more papers by this authorCorresponding Author
Hang Qi
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Correspondence
Hang Qi, School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian 116034, China.
Email: [email protected]
Search for more papers by this authorBaoyu He
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorYixin Shi
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorMeiran Jin
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorYuan Pu
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorXiuping Dong
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Search for more papers by this authorChenxu Yu
Department of Agricultural and Biosystems Engineering, Iowa State University, Ames, Iowa
Search for more papers by this authorCorresponding Author
Hang Qi
School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian, China
Correspondence
Hang Qi, School of Food Science and Technology, Dalian Polytechnic University, National Engineering Research Center of Seafood, Dalian 116034, China.
Email: [email protected]
Search for more papers by this authorFunding information: Dalian Science and Technology Foundation for Distinguished Young Scholars, Grant/Award Number: 2018RL07; The National Key Research and Development Program of China, Grant/Award Number: 2018YFD0400603; Young Top Talents Project of Liaoning Revitalization Talents Program, Grant/Award Number: XLYC1807166
Abstract
In this study, effects of different concentrations of riboflavin (0, 0.02, and 0.1 μmol/g protein) on myofibrillar protein (MP, Scomberomorus niphonius) gel were characterized. The gel structure and properties were studied with or without Ultraviolet A (UVA) irradiation. Electron spin resonance results showed that riboflavin produced ·OH under UVA irradiation, which subsequently oxidized the MP. Compared with the control group, the addition of riboflavin with UVA irradiation increased the strength of the MP gel. The rheological results showed that under UVA irradiation, addition of riboflavin facilitated the sol–gel transition between 45 and 52°C, indicating that oxidation led to significant structural changes which in turn resulted in a more compact and uniform gel network. The presence of riboflavin led to increased carbonyl content and decreased sulfhydryl and free amino groups, which decreased the protein solubility and promoted alpha-helical conformational loss in the secondary structure of the MP. These results all indicated that the MP has been oxidized. Electrophoresis revealed that myosin heavy chains were aggregated in the UVA-treated riboflavin-added MP gel, indicating that protein cross-linking has been induced. All the results indicated that the ·OH produced by riboflavin under UVA irradiation oxidized the MP, and improved protein crosslinking and gel properties.
CONFLICT OF INTEREST
The authors declare that there is no conflict of interest regarding the publication of this study.
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