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

doi:10.3390/foods11121705

Comparative Study on the Characterization of Myofibrillar Proteins from Tilapia, Golden Pompano and Skipjack Tuna

Foods. 2022 Jun 10;11(12):1705. doi: 10.3390/foods11121705.

Authors

Huibo Wang¹, Zhisheng Pei^{1

2}, Changfeng Xue², Jun Cao¹, Xuanri Shen^{1

3}, Chuan Li^{1

3}

Affiliations

¹ 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.
² School of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, China.
³ Collaborative Innovation Center of Provincial and Ministerial Co-Constructin for Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China.

Abstract

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.

Keywords: N-glycosylation; conformational structure; functional properties; myofibrillar proteins; physicochemical properties.

Grants and funding

This work was funded by the National Key R&D Program of China, grant number 2018YFD0901002; Hainan Provincial Natural Science Foundation of China, grant number 321RC747 and 320MS056; and the Innovation Platform for Academicians of Hainan Province, grant number YSPTZX202131.