Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates
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.
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Format: | artículo biblioteca |
Language: | English |
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Elsevier
2019-11-09
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Subjects: | Electrospinning, Pea protein isolate, Common bean protein isolate, Rheology, |
Online Access: | http://hdl.handle.net/10261/208761 http://dx.doi.org/10.13039/501100003141 |
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dig-iata-es-10261-2087612022-12-20T16:50:45Z Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates Aguilar-Vázquez, G. Ortiz-Frade, L. Figueroa-Cárdenas, J.D. López-Rubio, Amparo Mendoza, S. Consejo Nacional de Ciencia y Tecnología (México) Electrospinning Pea protein isolate Common bean protein isolate Rheology 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. This work was supported by the Universidad Autonoma de Queretaro (FOFI-UAQ2015 project) and by the Mexican National Council for Science and Technology (CONACYT, project No. 269102). Peer reviewed 2020-04-23T09:03:36Z 2020-04-23T09:03:36Z 2019-11-09 artículo http://purl.org/coar/resource_type/c_6501 Polymer Testing 81: 106217 (2020) 0142-9418 http://hdl.handle.net/10261/208761 10.1016/j.polymertesting.2019.106217 http://dx.doi.org/10.13039/501100003141 en Postprint https://doi.org/10.1016/j.polymertesting.2019.106217 Sí open Elsevier |
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Electrospinning Pea protein isolate Common bean protein isolate Rheology Electrospinning Pea protein isolate Common bean protein isolate Rheology |
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Electrospinning Pea protein isolate Common bean protein isolate Rheology Electrospinning Pea protein isolate Common bean protein isolate Rheology Aguilar-Vázquez, G. Ortiz-Frade, L. Figueroa-Cárdenas, J.D. López-Rubio, Amparo Mendoza, S. Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates |
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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. |
author2 |
Consejo Nacional de Ciencia y Tecnología (México) |
author_facet |
Consejo Nacional de Ciencia y Tecnología (México) Aguilar-Vázquez, G. Ortiz-Frade, L. Figueroa-Cárdenas, J.D. López-Rubio, Amparo Mendoza, S. |
format |
artículo |
topic_facet |
Electrospinning Pea protein isolate Common bean protein isolate Rheology |
author |
Aguilar-Vázquez, G. Ortiz-Frade, L. Figueroa-Cárdenas, J.D. López-Rubio, Amparo Mendoza, S. |
author_sort |
Aguilar-Vázquez, G. |
title |
Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates |
title_short |
Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates |
title_full |
Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates |
title_fullStr |
Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates |
title_full_unstemmed |
Electrospinnability study of pea (Pisum sativum) and common bean (Phaseolus vulgaris L.) using the conformational and rheological behavior of their protein isolates |
title_sort |
electrospinnability study of pea (pisum sativum) and common bean (phaseolus vulgaris l.) using the conformational and rheological behavior of their protein isolates |
publisher |
Elsevier |
publishDate |
2019-11-09 |
url |
http://hdl.handle.net/10261/208761 http://dx.doi.org/10.13039/501100003141 |
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