Molecular characterization of the effects of Ganoderma Lucidum polysaccharides on the structure and activity of bovine serum albumin.

The investigation about polysaccharides-protein system is attributed to numerous very important applications for pharmaceutical, food, chemical and other industries. In the present work, multi-spectral methods and molecular docking were used to analyze the molecular interactions of polysaccharides from Ganoderma Lucidum (GLP) with bovine serum albumin (BSA). The nonenzymatic glucosylation, fibrillation, thermal stability, and structure information of GLP-BSA system were also studied. The results showed that the formation of GLP-BSA complex by mainly hydrogen-bonding forces resulted in the conformational changes of protein. GLP acted as a stabilizer to increase the thermal stability of BSA solution having a novel and more stable conformational state during the thermal denaturation process. 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence spectral results suggested that there exist some intermediate state which has low binding ability with ANS in the presence of GLP. The presence of GLP caused a decrease in the formation of beta sheet structures with a lower rate. The fluorescence spectra of BSA glycosylated by GLP confirmed the formation of covalent bonds between BSA and GLP through the Maillard reaction which was also confirmed by using thermogravimetric (TGA) and Fourier transform infrared (FTIR) analysis. In addition, BSA still maintains the esterase-like good activity in the presence of GLP. These results provide a basis for screening the molecular interactions of polysaccharides with protein from the perspective of important food active ingredients.