LAUSR

Abstract Protein glycosylation results in structural changes which affects its functionalities. In this study, myofibrillar protein (MP) from pale, soft and exudative (PSE)-like chicken breast meat was grafted onto the glucosamine (GlcN) backbone using microbial transglutaminase (MTGase) as a biocatalyst and the impacts of glycosylation on structural and solubility properties of the conjugation product were investigated. The covalent attachment was verified by HPLC and Fourier transform infrared spectroscopy (FT-IR). The optimal conjugation conditions were 37 °C at pH 7.5 for 6 h with a MP to GlcN weight ratio of 1:3. The results of secondary structure analysis suggested that the glycosylated MP had decreased α-helix level and increased β-sheet, β-turns and random coil levels. After glycosylated with GlcN, the surface hydrophobicity was significantly reduced and the solubility of MP at the isoelectric point was markedly improved (P