Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8891012 | LWT - Food Science and Technology | 2018 | 35 Pages |
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 37â¯Â°C at pH 7.5 for 6â¯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 (Pâ¯<â¯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.
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Authors
Yujuan Xu, Xue Zhao, Guangliang Bian, Liu Yang, Minyi Han, Xinglian Xu, Guanghong Zhou,