2020
DOI: 10.1016/j.ultsonch.2019.104861
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Effect of ultrasound on binding interaction between emodin and micellar casein and its microencapsulation at various temperatures

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Cited by 46 publications
(49 citation statements)
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“…Comparably, the main interaction forces between tea polyphenols, rutin, and β-LG at neutral pH were dominated by hydrophobic interactions, which is similar to our results [2] , [9] . These data collaborated well with previous data showing that ultrasound may strengthen or weaken the interactions between dietary protein and phenolics, but would not alter the type of major driving forces [38] . Overall, ULG-35 showed the highest K a and ΔH values when interacting with EGCG/CA, thus was selected in the following experiments.…”
Section: Resultssupporting
confidence: 90%
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“…Comparably, the main interaction forces between tea polyphenols, rutin, and β-LG at neutral pH were dominated by hydrophobic interactions, which is similar to our results [2] , [9] . These data collaborated well with previous data showing that ultrasound may strengthen or weaken the interactions between dietary protein and phenolics, but would not alter the type of major driving forces [38] . Overall, ULG-35 showed the highest K a and ΔH values when interacting with EGCG/CA, thus was selected in the following experiments.…”
Section: Resultssupporting
confidence: 90%
“…Ultrasound pre-treatment was beneficial for the hydrophobic stacking interactions between β-LG and phenolics, and the form of β-LG (dimer/monomer) played a crucial role in the spatial structure of complexes due to the distinct binding locations [1] , [8] . A similar phenomenon of ultrasound-driven protein structural changes by phenolic binding was witnessed in EGCG/GA–egg white [5] and emodin–micellar casein systems [38] .…”
Section: Resultssupporting
confidence: 58%
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“…Crosslinking of casein micelles [110], was used to create casein nanoparticles using transglutaminase by pushing out micellar calcium phosphate. Recently, Yang and coworkers [134], investigated the microencapsulation of emodin, having antibacterial and potent antioxidant properties, in micellar casein by applying heat (25 • C, 30 • C, 37 • C) and ultrasound (20 kHz). Fluorescence evaluation revealed that the hydrophobic forces are the primary interaction between micellar casein and emodin while heating independent of ultrasounds.…”
Section: Researchers Cohen and Hahammentioning
confidence: 99%
“…11,12 Emodin is the major bioactive compound of R. officinale and has strong anti-inflammatory and antioxidant properties. 13 It has been reported that emodin notably suppresses the development of multiple diseases. 14,15 Additionally, it has previously been verified that emodin can relieve the progression of renal fibrosis.…”
Section: Introductionmentioning
confidence: 99%