Synthesis and structural characterization of lysozyme–pullulan conjugates obtained by the Maillard reaction

July 28, 2017

Title

Synthesis and structural characterization of lysozyme–pullulan conjugates obtained by the Maillard reaction

Author

Long Sheng, Peng Su, Ke Han, Jiahui Chen, Anqi Cao, Zhilong Zhang, Yongguo Jin, Meihu Ma

Year

2017

Journal

Food Hydrocolloids

Abstract

The purpose of this study was to produce lysozyme-pullulan conjugates under mild Maillard reaction conditions and investigate the influence of conjugation on structural and physical properties of the glycation product. The covalent attachment of pullulan to lysozyme was confirmed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum condition chosen for glycation was 60 °C at pH 7.5 for 5 days with a lysozyme to pullulan molar ratio of 1:8. Fluorescence and circular dichroism (CD) spectrum analysis suggested remarkable changes in the structure and conformation occurred to the lysozyme. The average particle size of glycosylated lysozyme was 3.5-fold to the native lysozyme and 2.4-fold to the heated lysozyme (P < 0.05). The surface hydrophobicity was greatly reduced and the solubility of lysozyme at different pH solutions was improved after covalent binding with pullulan (P < 0.05). Meanwhile, lysozyme-pullulan conjugates showed a broader range of antimicrobial activity than native lysozyme.

Instrument

J-1500

Keywords

Circular dichroism, Secondary structure, Thermal stability, Biochemistry, Food science