2016
DOI: 10.1016/j.foodchem.2016.06.017
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Physicochemical and functional properties of protein isolate produced from Australian chia seeds

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Cited by 177 publications
(143 citation statements)
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“…As shown in Table , compared with SCGs, the surface hydrophobicity of SCGPI was significantly reduced, while the total sulfhydryl groups and disulfide bonds were significantly increased, but the free sulfhydryl groups remained unchange. The comparison of surface hydrophobicity between SCGs and SCGPI was opposite to the solubility, which is similar to the results of the protein isolate from Australian chia seeds (Timilsena, Adhikari, Barrow, & Adhikaari, ). When the hydrophobic residue was exposed on the surface of the molecule, it is widely involved in the intermolecular interaction making the less solubility of the protein.…”
Section: Resultssupporting
confidence: 85%
“…As shown in Table , compared with SCGs, the surface hydrophobicity of SCGPI was significantly reduced, while the total sulfhydryl groups and disulfide bonds were significantly increased, but the free sulfhydryl groups remained unchange. The comparison of surface hydrophobicity between SCGs and SCGPI was opposite to the solubility, which is similar to the results of the protein isolate from Australian chia seeds (Timilsena, Adhikari, Barrow, & Adhikaari, ). When the hydrophobic residue was exposed on the surface of the molecule, it is widely involved in the intermolecular interaction making the less solubility of the protein.…”
Section: Resultssupporting
confidence: 85%
“…On the other hand, the addition of chia seeds increased the protein content proportional to the amount added. Chia seeds contain approximately 16.5% proteins, which is higher compared to the most commonly consumed grains such as wheat, barley, and oats (Timilsena et al., 2016; Valdivia‐López & Tecante, 2015). Studies have also shown that chia seeds contain both essential amino acids and non‐essential amino acids such as methionine, phenylalanine, cysteine, and glycine in significant amounts, giving it a high protein quality score (Ding et al., 2018; Nitrayová et al., 2014), and hence, it can be used to supplement low protein quality products such as pineapple jam.…”
Section: Discussionmentioning
confidence: 99%
“…Surface hydrophobicity of the samples was measured according the method explained by Timilsena et al (2016). The protein solution (1 mg/mL) was prepared in phosphate buffer (0.01 M, pH 7.0) and then centrifuged at 10,000g for 20 min to remove any insoluble matter.…”
Section: Surface Hydrophobicity Analysismentioning
confidence: 99%
“…EWP and WPI showed very high solubility (> 80%) at all studied pHs. Solubility of proteins in water depends on several factor including surface characteristics of their amino acids, molecular weight, and conformational situation (Timilsena et al 2016). For example, whey proteins are low molecular weight globular proteins remaining after pH-adjustment of milk to 4.6 during the casein coagulation process.…”
Section: Solubility Of Proteins In Watermentioning
confidence: 99%
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