Comparative Study on the Characterization of Myofibrillar Proteins from Tilapia, Golden Pompano and Skipjack Tuna
Huibo Wang,
Zhisheng Pei,
Changfeng Xue,
Jun Cao,
Xuanri Shen,
Chuan Li
Affiliations
Huibo Wang
Hainan Provincial Engineering Research Centre of Aquatic Resources Efficient Utilization in the South China Sea, School of Food Science and Engineering, Hainan University, Haikou 570228, China
Zhisheng Pei
Hainan Provincial Engineering Research Centre of Aquatic Resources Efficient Utilization in the South China Sea, School of Food Science and Engineering, Hainan University, Haikou 570228, China
Changfeng Xue
School of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, China
Jun Cao
Hainan Provincial Engineering Research Centre of Aquatic Resources Efficient Utilization in the South China Sea, School of Food Science and Engineering, Hainan University, Haikou 570228, China
Xuanri Shen
Hainan Provincial Engineering Research Centre of Aquatic Resources Efficient Utilization in the South China Sea, School of Food Science and Engineering, Hainan University, Haikou 570228, China
Chuan Li
Hainan Provincial Engineering Research Centre of Aquatic Resources Efficient Utilization in the South China Sea, School of Food Science and Engineering, Hainan University, Haikou 570228, China
In this study, the physicochemical properties, functional properties and N-glycoproteome of tilapia myofibrillar protein (TMP), golden pompano myofibrillar protein (GPMP) and skipjack tuna myofibrillar protein (STMP) were assessed. The microstructures and protein compositions of the three MPs were similar. TMP and GPMP had higher solubility, sulfhydryl content and endogenous fluorescence intensity, lower surface hydrophobicity and β-sheet contents than STMP. The results showed that the protein structures of TMP and GPMP were more folded and stable. Due to its low solubility and high surface hydrophobicity, STMP had low emulsifying activity and high foaming activity. By N-glycoproteomics analysis, 23, 85 and 22 glycoproteins that contained 28, 129 and 35 N-glycosylation sites, were identified in TMP, GPMP and STMP, respectively. GPMP had more N-glycoproteins and N-glycosylation sites than STMP, which was possibly the reason for GPMP’s higher solubility and EAI. These results provide useful information for the effective utilization of various fish products.
