Location: Cereal Crops ResearchTitle: Supercritical fluid extraction as a deodorization tool: Effect on pea protein isolate properties
|VATANSEVER, SERAP - NORTH DAKOTA STATE UNIVERSITY|
|SIMSEK, SENAY - NORTH DAKOTA STATE UNIVERSITY|
|HALL, CLIFFORD - SOUTH DAKOTA STATE UNIVERSITY|
Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 1/31/2020
Publication Date: N/A
Interpretive Summary: .
Technical Abstract: Dry pea (Pisum sativum L.) is an excellent source of protein that has a high lysine content. However, pea proteins have limited applications in the food industry due to the undesirable flavor. This study aimed to determine the effects of supercritical fluid extraction (SFE), as a deodorization method, on functional, structural, thermal, and morphological properties of pea protein isolate (PPI) extracted from deodorized pea flour. Moisture, protein, ash, and total starch content of native PPI (NPPI) and deodorized PPI (DPPI) were tested. Protein solubility, emulsion and foaming properties, and color values of PPI were determined. Thermal properties, structural characteristics, protein composition, morphological structure of protein samples were analyzed using differential scanning calorimetry (DSC), Fourier transform infrared (FTIR) spectroscopy and X-ray diffraction (XRD), Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), and scanning electron microscopy (SEM), respectively. Moisture (6.1%), protein (82.8%), total starch (7.7%) of DPPI were significantly (p < 0.05) higher and resulted in lighter isolate than that of NPPI. Denaturation temperature (92.7 C) of vicilin from DPPI was higher than for NPPI. Protein solubility, emulsion capacity (502%) and stability (43%) at pH 7, and foaming capacity and stability at different pH of DPPI were significantly higher than the respective values in NPPI. SPS-PAGE profile showed DPPI had four different individual proteins compared to NPPI. SEM image of DPPI showed the presence of starch granules and smaller protein layers. The FTIR spectra of DPPI had a strong peak at 1051 cm–1, which was associated with occurrence starch. NPPI had two different peaks at 1739 cm–1 (ester C=O stretch) and at 2854 cm–1 (CH2 stretch) for lipids, which were not present in DPPI. XRD patterns were similar between NPPI and DPPI. SFE had prominent impacts on the proximate composition, structure, functionality, thermal characteristics, and morphologic structure of DPPI. The results support that this extraction improved functionality of PPI and supports SFE as a green technology to modify plant proteins such as pea protein. The added benefit includes reduction of lipid.