A Study On The Mechanism Of Wheat Glutenin-carboxymethyl Cellulose Self-assembly And Its Delivery Property

Today’s scientific diet pursues a balanced,healthy,low-carbon,green and environmentally friendly diet,for which plant-based proteins have many advantages over animal-derived proteins.However,many plant-based proteins,such as rice protein,zein and wheat glutenin,have unfavorable processing performance due to poor water diversity.This has been a challenge for the widespread industrial application of highly hydrophobic plant-based proteins.Based on the principle of molecular chaperone,this study investigates the p H-cycle mediated pathway and technology for the hydrophilic co-folding and self-assembly of proteins and polysaccharides,with the aim to improve the water dispersity of plant-based proteins,focusing on the principles and methods of integrating and balancing the forces between proteins and polysaccharides.Based on this,the potential of protein-polysaccharide complex for delivering hydrophobic active substances is examined.The pH-cycle mediated method of hydrophobic protein-water soluble polysaccharide network composite structures（CWs）and their application properties.The p H-cycle-mediated highly water-dispersible CWs of carboxymethyl cellulose（CMC）with wheat glutenin（WGs）were obtained.CWs had a beaded network microstructure,in which larger-sized WGs nanoparticles（～160 nm）were immobilized at the junctions of the CMC fiber network（～50 nm in thickness）,while many smaller-sized WGs nanoscale particles were attached to the CMC fiber backbone.Intrinsic fluorescence and Fourier transform infrared spectroscopy indicated that electrostatic interactions initiated the binding of WGs to CMC,while hydrophobic interactions promoted the growth of WGs nanoparticles on CMC fibers.More importantly,the microstructure of CWs can be precisely regulated by the degree of substitution（DS）of CMC.the CWs microstructure allowed the WGs to be fully dispersed in water,while the WGs nanoparticles can act as the binding site of VD₃ for efficient loading of VD₃（VD₃@CWs）.The temperature stability and UV radiation stability of VD₃ were improved by 77.87%to 92.55%and 113.13%to 166.45%,respectively,which were also highly correlated with DS.In addition,VD₃ had controlled sustained release properties in in vitro simulated gastrointestinal digestion experiments.The results of this study innovate the technical route of WGs utilization.The dynamic process of binding and the mechanism of complex formation.A sequential model of p H-mediated protein-polysaccharide interactions was developed based on p H-cycle-mediated dynamic simulations of the binding process between WGs and CMC on quartz crystal microbalance（QCM）.The binding of WGs and CMC mainly occurred at p H 10.0～p H 8.0,indicating that the electrostatic interaction between the two was the main driver of their binding.This hypothesis was further verified by single-point binding experiments,where the binding of WGs to CMC increased from 0.60±0.04 ng/ng pro to 1.59±0.14 ng/ng pro as the DS increased from 0.7 to 1.2,which was consistent with the trend of the flexibility of the adsorbed layer.The thermodynamic parameters indicated that the binding of WGs to CMC was a spontaneous exothermic reaction driven by enthalpy.The binding kinetics of WGs to CMC was equally affected by the synergistic effect of p H and DS.Moreover,different salt ions could inhibit the binding behavior of WGs with CMC,confirming the electrostatic mechanism of interaction between them.Therefore,the sequential interaction model developed based on QCM can provide a new practical pathway to study similar dynamic reaction processes.