Oat protein isolate (OPI)is amongtheplant proteins with valuable functionalities (e.g.emulsification)during daily supplement intake. Understanding their structures helps to manipulate oat proteins at small scale, which enables the appropriate deployment of their functions.Based upon such understanding, the molecular structure of oat protein isolate (OPI)in aqueous mediumwas investigated by synchrotron small-angle X-ray scattering (SAXS), and this study allows a structural reconstitution of OPI in aqueous medium. Besides, this SAXS study is complimentary to the previous study (Liu et al. J. Agric. Food Chem. 2009, 57, 4552–4558)[1].From form factor fitting, we confirmed that OPI aqueous solutions at low concentrations (0.3~2 mg/mL) obtained a disk conformation (41.4×41.4×10.2 Å3). Once protein concentration increased to 5 mg/mL and 10 mg/mL, the individual disk proteins formed large-dimensional rod-like aggregates, which was evidenced by the analyses of effective structure factorand pair distribution function (PDF). Based on the PDF results, the ab initio models of OPI particles at low concentrations (0.3 mg/mL to 2.0 mg/mL) were restored by using GASBOR algorithm. Finally, we found that weak attraction between OPI particles occurred, which was verified by second virial coefficientand pair potential.
Structural Investigation of Oat Protein Isolate in Aqueous Medium by using Synchrotron Small-angle X-ray Scattering
- Ji Li
- Qingrong Huang
Ji Li
Nutraceutical Corporation, 1777 Sun Peak Dr., Park City, Utah 84098
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Qingrong Huang
Department of Food Science, Rutgers University, 65 Dudley Road, New Brunswick, New Jersey 08901-8520, U.S.A.
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Cite this:
Ji Li, & Qingrong Huang. (2020). Structural Investigation of Oat Protein Isolate in Aqueous Medium by using Synchrotron Small-angle X-ray Scattering. Journal of Medical Biomedical and Applied Sciences, 8(11), 535–547. https://doi.org/10.15520/jmbas.v8i11.258
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