Effects of heat treatment on physicochemical and microstructure properties of myofibrillar proteins combined with glucose and cellulose nanofibers

The effects of unheated, 80 degrees C, 100 degrees C, and 121 degrees 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 degrees C and 100 degrees C, the particle size and hydrophobicity of MP significantly increased. At 121 degrees 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 degrees C).

Automated summary

This study investigated the effects of different temperatures on the physicochemical and microstructural properties of myofibrillary protein supplemented with glucose and cellulose nanofibers. The results showed that glucose and cellulose nanofibers could cross-link with myofibrillary protein through non-covalent bonds, leading to changes in the structure and properties of myofibrillary protein. The particle size and hydrophobicity of myofibrillary protein were found to change at different temperatures. At 121 degrees C, the addition of glucose and cellulose nanofibers prevented the loss of leucine and lysine in myofibrillary protein. Microscopic images revealed better dispersion of glucose-myofibrillary protein and cellulose nanofibers-myofibrillary protein.