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Title: Structure, morphology, and assembly behavior of kafirin

Abstract

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, andmore » disk-like or rod-like structures resulting from solvent evaporation induced particle interactions emerged at high concentrations. Lastly, 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.« less

Authors:
 [1];  [2];  [1];  [1];  [1];  [1]
  1. Rutgers Univ., New Brunswick, NJ (United States)
  2. Changchun Institute of Applied Chemistry, Changchun (People's Republic of China)
Publication Date:
Research Org.:
Rutgers Univ., New Brunswick, NJ (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1346014
Grant/Contract Number:  
AC02-06CH11357
Resource Type:
Accepted Manuscript
Journal Name:
Journal of Agricultural and Food Chemistry
Additional Journal Information:
Journal Volume: 63; Journal Issue: 1; Journal ID: ISSN 0021-8561
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; 59 BASIC BIOLOGICAL SCIENCES; kafirin; morphology; SAXS; SDS-PAGE; secondary structure; self-assembly

Citation Formats

Xiao, Jie, Li, Yunqi, Li, Ji, Gonzalez, Alejandro Perez, Xia, Qiuyang, and Huang, Qingrong. Structure, morphology, and assembly behavior of kafirin. United States: N. p., 2014. Web. doi:10.1021/jf504674z.
Xiao, Jie, Li, Yunqi, Li, Ji, Gonzalez, Alejandro Perez, Xia, Qiuyang, & Huang, Qingrong. Structure, morphology, and assembly behavior of kafirin. United States. https://doi.org/10.1021/jf504674z
Xiao, Jie, Li, Yunqi, Li, Ji, Gonzalez, Alejandro Perez, Xia, Qiuyang, and Huang, Qingrong. Mon . "Structure, morphology, and assembly behavior of kafirin". United States. https://doi.org/10.1021/jf504674z. https://www.osti.gov/servlets/purl/1346014.
@article{osti_1346014,
title = {Structure, morphology, and assembly behavior of kafirin},
author = {Xiao, Jie and Li, Yunqi and Li, Ji and Gonzalez, Alejandro Perez and Xia, Qiuyang and Huang, Qingrong},
abstractNote = {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. Lastly, 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.},
doi = {10.1021/jf504674z},
journal = {Journal of Agricultural and Food Chemistry},
number = 1,
volume = 63,
place = {United States},
year = {Mon Dec 15 00:00:00 EST 2014},
month = {Mon Dec 15 00:00:00 EST 2014}
}

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