Foods (Apr 2023)

Transglutaminase-Catalyzed Glycosylation Improved Physicochemical and Functional Properties of <i>Lentinus edodes</i> Protein Fraction

  • Shan-shan Wu,
  • Wei Han,
  • Yan-fen Cheng,
  • Shao-jun Yun,
  • Ming-chang Chang,
  • Fei-er Cheng,
  • Jin-ling Cao,
  • Cui-ping Feng

DOI
https://doi.org/10.3390/foods12091849
Journal volume & issue
Vol. 12, no. 9
p. 1849

Abstract

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Lentinula edodes has high nutritional value and abundant protein. In order to develop and utilize edible mushroom protein, this study was designed to investigate the effects of TGase-catalyzed glycosylation and cross-linking on the physicochemical and functional properties of Lentinus edodes protein fraction. The results showed that within a certain time, glycosylation and TGase-catalyzed glycosylation decreased the total sulfydryl, free sulfydryl, disulfide bond, surface hydrophobicity, β-fold and α-helix, but increased the fluorescence intensity, random coil, β-turn, particle size and thermal stability. The apparent viscosity and the shear stress of the protein with an increase in shear rate were increased, indicating that TGase-catalyzed glycosylation promoted the generation of cross-linked polymers. In addition, the TGase-catalyzed glycosylated proteins showed a compact texture structure similar to the glycosylated proteins at the beginning, indicating that they formed a stable three-dimensional network structure. The flaky structure of proteins became more and more obvious with time. Moreover, the solubility, emulsification, stability and oil-holding capacity of enzymatic glycosylated Lentinus edodes protein fraction were significantly improved because of the proper TGase effects of glycosylation grafting and cross-linking. These results showed that glycosylation and TGase-catalyzed glycosylation could improve the processing characteristics of the Lentinula edodes protein fraction to varying degrees.

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