Differentiation of glycated residue numbers on heat-induced structural changes of bovine serum albumin.

Abstract

Glycation is an approach in dealing with heat-induced protein aggregation. The relationship between degree of glycation and heat-induced structural changes is still unclear. The present work investigates the effect of different numbers and sites of glycated residues on heat-induced structural changes of bovine serum albumin (BSA). Glycation of BSA was carried out with xylose (Xyl) and galactose (Gal) by Maillard reaction. Glycated residues in BSA were identified by liquid chromatography-tandem mass spectrometry, and heat-induced protein structural changes were characterized by fluorescence emission and synchronous fluorescence spectra, 8-anilino-1-naphthalenesulfonic acid fluorescence, Fourier transform infrared (FTIR) and circular dichroism (CD) spectra. The numbers of glycated residues were 2 and 13 when BSA was glycated by Gal (BSA - Gal) and Xyl (BSA - Xyl), respectively. There were shifts of maximum wavelengths and decreases in fluorescence intensities for both intrinsic and extrinsic fluorescences; shifts of FTIR amide I, III, and A bands; and decrease or increase of CD band intensities, α-helix and β-sheet percentages when BSA was heated. Glycation with Gal or Xyl restrained in similar degrees those changes, including fluorescence wavelengths, amide I band, CD band intensities, and α-helix and β-sheet percentages. Xyl glycated more residues than Gal, while their effects were similar in restraining heat-induced BSA structural changes. © 2017 Society of Chemical Industry.