2022
DOI: 10.1016/j.ultsonch.2022.106232
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Impacts of sonication and high hydrostatic pressure on the structural and physicochemical properties of quinoa protein isolate dispersions at acidic, neutral and alkaline pHs

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Cited by 20 publications
(10 citation statements)
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“…The amide I band (1600–1700 cm −1 ) primarily represents the C O stretching vibrations of the peptide linkages, and is regarded as the fingerprint for the secondary structural components of proteins [31] , [58] . Therefore, the characteristic peaks of the amide I band were used to quantitatively analyze the secondary structural elements of proteins, including α-helix, β-turn, β-sheet, and random coil ( Table 4 ).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…The amide I band (1600–1700 cm −1 ) primarily represents the C O stretching vibrations of the peptide linkages, and is regarded as the fingerprint for the secondary structural components of proteins [31] , [58] . Therefore, the characteristic peaks of the amide I band were used to quantitatively analyze the secondary structural elements of proteins, including α-helix, β-turn, β-sheet, and random coil ( Table 4 ).…”
Section: Resultsmentioning
confidence: 99%
“…The color of the crayfish samples was measured using a CM-700d spectrophotometer (Konica Minolta, Shanghai, China) with standard blackboard zeroing and calibrated with a standard white plate, according to the method in Wei et al [31] . The samples were selected from the 2nd to 3rd abdominal segments of crayfish tails for analysis.…”
Section: Methodsmentioning
confidence: 99%
“…The adsorption of bile acids, hydrophobic substances, depends on hydrophobic and electrostatic interactions. However, ultrasound treatment exposed a large number of hydrophilic groups in protein and dietary fiber [ 80 , 82 ], resulting in a significant decline in the BBC.…”
Section: Resultsmentioning
confidence: 99%
“…Regarding functional properties, the surface hydrophobicity of proteins subjected to HHP exhibited variations ( Table 1 ). Millet protein [ 23 ] and quinoa protein [ 27 ] demonstrated a decrease in this property after being treated at 500–600 MPa for 10–15 min, while rice proteins [ 19 , 24 ] and wheat protein [ 17 ] exhibited an increase at >300 MPa. This disparity was found to be associated with changes in fluorescence intensity.…”
Section: Effects Of Hhp On Allergenicity Bioactivities As Well As Str...mentioning
confidence: 99%
“…Additionally, the reduced hydrophobicity resulted from protein aggregation, with HHP exposing buried tryptophan residues to the microenvironment, thereby triggering aggregation. Protein aggregation was further evidenced by an increase in particle size and a reduction in zeta potential in millet protein [ 23 ] and quinoa protein [ 27 ], impacting structural forms. The decrease in α-helix content converted to β-sheets contributed to a decline in surface charge and electrostatic repulsion, further promoting protein aggregation [ 23 ].…”
Section: Effects Of Hhp On Allergenicity Bioactivities As Well As Str...mentioning
confidence: 99%