Abstract: In order to develop and utilize Lentinus edodes protein, the effect of glutamine transaminase (TGase) cross-linking on the physicochemical and processing characteristics of L. edodes protein was studied. The results showed that the addition of 0%–20% TGase gradually reduced the contents of total thiol, free thiol and β-sheet of L. edodes protein, while the fluorescence intensity, particle size, β-turn content and surface hydrophobicity showed a trend of initially increasing and then decreasing. As the shear rate increased, the shear stress of the protein increased and the apparent viscosity decreased, indicating that TGase cross-linking promoted the generation of macromolecular polymers. In addition, the cross-linked protein exhibited a dense texture similar to that of the original protein, indicating the formation of a stable three-dimensional network structure. As the addition level of TGase increased from 4% to 12%, the protein network structure became increasingly dense. Moreover, an appropriate amount of TGase significantly improved the solubility, emulsifying properties, thermal stability, and oil-holding capacity of L. edodes protein. These results indicate that TGase cross-linking improves the physicochemical and processing properties of L. edodes protein to varying degrees.

Key words: Lentinus edodes protein; glutamine transaminase; physicochemical properties; processing characteristics