小麦醇溶蛋白肽凝胶制备及其结构特性OA

To explore the self-assembly gelation behavior of wheat gliadin peptides and develop novel plant-based func-tional gel materials,the targeted peptide segment was acquired via ultra-filtration through the controlled enzymatic hydrol-ysis of gliadin by alkaline protease in this study.A series of multi-scale characterization methods,including texture profile analysis,rheometry,scanning electron microscopy(SEM),atomic force microscopy(AFM),Zeta potential analysis,FT-IR spectroscopy,hydrophobicity determination,disulfide bond determination,and so on were comprehensively employed to assess its physico-chemical property,micro-structure and molecular mechanism.According to the findings,the molecular weight of gliadin peptide ranged predominantly from 1 to 5 kDa.This peptide segment could form a stable gel at a concen-tration of 15%,and its hardness increased with concentration.Its rheological behavior showed shear-thinning characteris-tics;SEM and AFM revealed that the gel featured regular porous structure and uniform nano-spheric morphology;Zeta potential analysis(-43.63±1.41 mV)indicated an excellent colloidal stability.In terms of molecular mechanism,FT-IR spectroscopy confirmed the hydrogen bonding as its primary driving force,with the increased α-helix content(25.1%→37.9%)representing the crucial conformational transition.Hydrophobic interaction and disulfide bond exchange jointly promoted assembly.Sequence analysis revealed typical amphiphilic arrangement patterns of(XZXZ)n and(UCUC)n.This study has innovatively elucidated the mechanism by which gliadin peptide forms a stable self-assembled gel via hydrogen-bond-dominated molecular forces.It provides both a theoretical basis and a material foundation for professionals to apply the plant peptide-based gel into food texture profile improvement and pharmaceutical delivery vector development.