LAUSR

BACKGROUND Soybean 11S globulin has good functional properties, which widely used in the field of food. However, natural soybean 11S globulin (N-11S) has low flexibility and easy to aggregate, which impact its foaming process. Studies have shown that molten globule state soybean 11S globulin (MG-11S) has better molecular flexibility than N-11S, and trehalose has been shown to improve the properties of proteins. Therefore, this study investigated the interaction mechanism between trehalose and MG-11S, and its impact on rheological and foaming properties of MG-11S. RESULTS The molecular docking and intrinsic fluorescence results showed that hydrogen bonding was the main interaction force at lower 0.5 mol L-1 trehalose added, meanwhile rheology and foaming showed that the MG-11S-trehalose complexes had better viscoelasticity, foaming ability (66.67%-86.67%) and foaming stability (75.00%-89.29%) than those of N-11S (16.67% of foaming ability and 40.00% of foaming stability); however, when the trehalose was higher than 0.5 mol L-1 , molecular crowding occurred and weaken H-bonds, resulting in reduction of foaming capacities. The microstructure determination observed that trehalose attached to the surface of foam membrane; meanwhile the foaming structure of the complex with 0.5 mol L-1 trehalose had a thicker liquid film with decreased drainage rate, less agglomeration and disproportionation of foam, illustrating the best foaming ability and foaming stability. CONCLUSIONS The results suggested that trehalose with different concentrations can interact with MG-11S through different mechanisms, and improve the foaming capacities of MS-11S. This provided a reference for the application of the MS-11S in foaming food. This article is protected by copyright. All rights reserved.