Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates

• Published in: Polymer testing 2020-01, Vol.81, p.106217, Article 106217
• Main Authors: Aguilar-Vázquez, G., Ortiz-Frade, L., Figueroa-Cárdenas, J.D., López-Rubio, A., Mendoza, S.
• Format: Article
• Language: English
• Subjects: Common bean protein isolate; Electrospinning; Pea protein isolate; Rheology
• ISSN: 0142-9418; 1873-2348
• DOI: 10.1016/j.polymertesting.2019.106217

Pea protein isolate (PPI) and bean protein concentrate (BPC) were evaluated as fiber-forming vegetal source materials through electrospinning using various solvents. The effects of hexafluoroisopropanol (HFIP), trifluoroethanol (TFE), trifluoroacetic acid (TFA), formic acid (FA) and water on rheological and conformational properties of the protein solutions were determined. The morphology and molecular organization of the electrospun structures were studied. All PPI and BPC solutions displayed pseudoplastic behavior. Circular dichroism spectroscopy revealed that β-type turns and β-sheets were the dominant protein conformations in water, HFIP, and TFE. After electrospinning, most of the solutions afforded beads. Fiber-like morphologies were only obtained when BPC was dissolved in HFIP. BPC demonstrated better performance in the electrospinning process than PPI. Denaturation of the protein isolates was not sufficient to form fibers, the viscosity of the solution as well as the vapor pressure of the solvents played an important role in defining the morphology. [Display omitted] •Solutions of protein isolates in HFIP, TFE, TFA and FA showed a pseudoplastic behavior.•Beads were the most common morphology of the electrospun structures.•BPC demonstrated better performance in the electrospinning process than PPI.•BPC electrospun structures were obtained for the first time.