Structure, Morphology, and Assembly Behavior of Kafirin

Xiao, Jie; Li, Yunqi; Li, Ji; Gonzalez, Alejandro Perez; Xia, Qiuyang; Huang, Qingrong

doi:10.1021/jf504674z

Title: Structure, Morphology, and Assembly Behavior of Kafirin

Journal Article · Wed Jan 14 00:00:00 EST 2015 · Journal of Agricultural and Food Chemistry

DOI:https://doi.org/10.1021/jf504674z· OSTI ID:1351364

Xiao, Jie; Li, Yunqi; Li, Ji; Gonzalez, Alejandro Perez; Xia, Qiuyang; Huang, Qingrong

Prolamins from grains have attracted intensive attention in recent years due to their potential in satisfying the demand for environmentally friendly (biodegradable), abundantly available (sustainable), and cost-effective biomaterials. However, for kafirin, the prolamin from sorghum, its composition, structure, morphology, and self-assembly behaviors have not been fully characterized. In this paper, kafirin was extracted from the whole sorghum grain and found to contain 68, 14, 6, and 12% of α-, β-, and γ-fractions and cross-linked kafirin, respectively. Freeze-dried kafirin contained ~49% α-helix in the solid state. When dissolved in 65% (v/v) isopropanol, 60% (v/v) tert-butanol, and 85% (v/v) ethanol aqueous solvents, the relative α-helix content in kafirin increased with the decrease of solvent polarity. Structural analysis using small-angle X-ray scattering (SAXS) indicated that kafirin (2 mg/mL) took stretched and extended conformations with dimensions of 118 × 15 × 15 and 100 × 11 × 11 Å in 60% tert-butanol and 65% isopropanol, respectively. More elongated conformation of individual kafirin with high-order assembly was observed in 85% ethanol. Protein aggregation occurred as protein concentration increased in its good solvent. The morphology of kafirin assemblies captured by atomic force microscopy (AFM) revealed that kafirin protein took uniform particle morphology at low concentration, and disk-like or rod-like structures resulting from solvent evaporation induced particle interactions emerged at high concentrations. These results suggest that both protein concentration and solvent polarity can effectively regulate kafirin assemblies from thick rod-like to slim rod-like structures, a convenient way to tune the fibrillation of prolamin-based biomaterials.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

OSTI ID:: 1351364

Journal Information:: Journal of Agricultural and Food Chemistry, Vol. 63, Issue 1; ISSN 0021-8561

Publisher:: American Chemical Society

Country of Publication:: United States

Language:: ENGLISH

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