To develop high value-added materials from agricultural by-products, continuous ultra-fine fibers with average diameters of 184.1 and 192.4 nm were successfully electrospun from hordein and gliadin and compared with that of zein for the first time. The relationships between protein conformation in solution and structures of post-spun fibers were investigated. The results revealed that, although these prolamin proteins exhibited similar amino acid compositions, their conformation in solution and electrospinnability were quite different. The change of conformation from compact to extended structures led to lowered and narrowed electrospinnable protein concentration and the transition from individual fibers to adherent ones. Moreover, hordein fibers were found to have much lower cytotoxicity (cell viability of 83.4%) than gliadin and zein fibers (56.0 and 66.1%). This fundamental work not only allows insight into inherent features that affect the manufacture of prolamin protein based nanofibers, but also suggests the potential applications of hordein fibers in food and pharmaceutical fields.

Fabrication and characterization of prolamin protein based electrospun nanofibers: Structure and biocompatibility

243rd National Meeting (2012)

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