Abstract
The understanding of the protein structure-function relationship is very important to the study of protein chemistry. In this research, the physicochemical, functional, and structural properties of the storage protein fractions from two defatted proso millet cultivars (Dawn and Plateau) were determined and reported. The results show that protein recovery efficiency of 53.5% and 60.1% was recorded for Dawn and Plateau, respectively. The average denaturation temperature of all fractions was about 82.1 ± 3.5 °C. Surface hydrophobicity values for Dawn fractions were 11781, 10594, 316, and 2225 for albumin, globulin, and glutelin, respectively and 3415, 2865, 353, and 456 for Plateau fractions, respectively. Most of the protein fractions showed the highest solubility at pH 9 and lowest solubilities at pH ≤ 7 with solubility range from 5.7 to 100%. Emulsifying activity index (EAI) of less than 0.25 m2/g was recorded for most fractions, while the highest emulsion stability index (ESI) recorded was about 60 min. Prolamin fractions showed three major peptide bands of 11, 14, and 24 kDa while glutelin fraction revealed only a major band of 15 kDa and several minor bands of 11, 22, 24, 78, 209 kDa. No differences in the electrophoresis pattern were observed for the fraction with or without a reducing agent.
Original language | English |
---|---|
Article number | 105497 |
Journal | Food Hydrocolloids |
Volume | 108 |
DOIs | |
State | Published - Nov 2020 |
Bibliographical note
Funding Information:This work was supported by the Kentucky Agricultural Experiment Station (KAES) , and the National Institute of Food and Agriculture (NIFA), U.S. Department of Agriculture , Hatch- Multistate project #: 1007893 . Additionally, authors are grateful to Dr. Konstantin V. Korotkov of the Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, USA for the use of his laboratory for some proteomic study.
Funding Information:
This work was supported by the Kentucky Agricultural Experiment Station (KAES), and the National Institute of Food and Agriculture (NIFA), U.S. Department of Agriculture, Hatch- Multistate project #: 1007893. Additionally, authors are grateful to Dr. Konstantin V. Korotkov of the Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, USA for the use of his laboratory for some proteomic study.
Publisher Copyright:
© 2019 Elsevier Ltd
Keywords
- Emulsion
- Foam
- Proso millet
- Protein fractions
- Solubility
ASJC Scopus subject areas
- Food Science
- Chemistry (all)
- Chemical Engineering (all)