Behavior of bovine serum albumin in the presence of locust bean gum.

In the present work, we have studied the structure and thermal stability of bovine serum albumin (BSA)-locust bean gum (LBG) mixture. It was found from the spectral results that the presence of LBG resulted in slightly decreasing the α-helical content and the partly unfolding of the skeleton of BSA. LBG binds to the neighboring amino acids of Trp and partly disturbs the microenvironment around Trp residues of BSA. The molecular docking confirms that there are more than one possible binding sites to bind with LBG by multi non-covalent forces. During the thermal unfolding process, LBG led to increase the secondary structure stability of protein by assembling each other. In addition, BSA even has good reversibility of the unfolding process in the presence of LBG promoting the thermal-induced tertiary structural degeneration of BSA. Collectively, our results provide evidence that LBG induces some behavior changes of BSA.