Structural and solubility properties of pale, soft and exudative (PSE)-like chicken breast myofibrillar protein: Effect of glycosylation

摘要

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 degrees C at pH 7.5 for 6 h with a MP to GleN weight ratio of 1:3. The results of secondary structure analysis suggested that the glycosylated MP had decreased alpha-helix level and increased beta-sheet, beta-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 & 0.05). Overall, the information obtained from this study can enrich the theoretical frame of enzymatic glycosylation. Additionally, these results suggest that enzymatic glycosylation is a promising approach for improving the solubility of MP from PSE-like chicken breast meat for food applications.