Abstract
The effects of unheated, 80 °C, 100 °C, and 121 °C on the physicochemical and microstructural properties of myofibrillary protein (MP) supplemented with glucose (Glc) and cellulose nanofibers (CNFs) were studied. The results showed that Glc and CNFs cross-linked with MP through non-covalent bonds when unheated compared with the unheated MP group, which increased the particle size and surface hydrophobicity of MP, and changed the secondary structure. At 80 °C and 100 °C, the particle size and hydrophobicity of MP significantly increased. At 121 °C, the contents of leucine and lysine in MP decreased by 16.2% and 19.9%, respectively, however, both Glc and CNFs could prevent this decrease. Meanwhile, microscopic images showed that the dispersion of Glc-MP and CNFs-MP were more uniform than the MP groups. Compared with Glc-MP, CNFs-MP had more uniform particle size distribution and better thermal stability at high temperatures (121 °C).
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