Abstract
ABSTRACTIn this study, cumin protein isolates (CPI) and major protein fractions were extracted and separated from cumin seeds, their structure, physicochemical, and functional properties were investigated. Albumin (62.29%) and glutelin (25.16%) were the predominant protein fractions of cumin seeds. Glutamic acid (Glu) and aspartic acid (Asp) were the major amino acids of cumin proteins, whereas more hydrophobic and aromatic amino acids were predominantly found in chickpea protein isolates. Electrophoresis profiles indicated that CPI have more disulphide bonds than major protein fractions. The intrinsic fluorescence data revealed that glutelin displayed greater exposure of tyrosine (Tyr) and tryptophan (Trp) residues compared to albumin and CPI. Circular dichroism (CD) data showed CPI presented more α-helix (14.4%) and less β-strand (30.7%) than albumin and glutelin. The atomic force microscope (AFM) profile and hydrodynamic diameter (Dh) determination showed the presence of low particle size in albumin fractions. Differences in the hydrophobicity (Ho) and the zeta-potential (ζ) of CPI, albumin, and glutelin were also observed due to their difference in structure and amino acid composition. Compared with CPI and glutelin, albumin exhibited the highest emulsifying activity (103.67 m2/g) and stability (42.84 min) and the smallest emulsion particle size (4.29 μm). The CPI, albumin and glutelin presented typical U-shaped protein solubility–pH curves, with the lowest solubility at pH 4.0. Rheological investigation demonstrated that CPIs were efficient in forming a gel at 80.6°C, whereas glutelin could form the hardest gel at 92.6°C. The overall results suggested that the cumin proteins can be a promising protein source for the food industry.
Highlights
IntroductionPlant proteins are widely studied and used in the food industry, such as soybean protein[1,2], chickpea protein[3], kidney bean protein[4], and peanut protein.[5] Commonly, plant proteins are divided into four categories – albumin, globulin, prolamin, and glutelin – according to their solubility in different solvents, such as water, salt, alcohol, and alkali solution.[6] Different ratios of those four categories are found in various plants
Protein is a major nutritional source for human and animals
This study investigated the main protein fractions presented in cumin seed as well as the structure, physicochemical, and functional properties of the protein isolate and the major protein fractions from cumin seed
Summary
Plant proteins are widely studied and used in the food industry, such as soybean protein[1,2], chickpea protein[3], kidney bean protein[4], and peanut protein.[5] Commonly, plant proteins are divided into four categories – albumin, globulin, prolamin, and glutelin – according to their solubility in different solvents, such as water, salt, alcohol, and alkali solution.[6] Different ratios of those four categories are found in various plants. Globulin has higher contents in aromatic and hydrophobic residues and more disulphide bonds than albumin, but the solubility and foaming capacity of albumin are higher than those of globulin.[9] The protein fractions from pumpkin seed showed significantly
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