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2019
DOI: 10.1016/j.ifset.2019.03.006
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Effects of dielectric barrier discharge plasma on the physicochemical and functional properties of myofibrillar proteins

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Cited by 75 publications
(35 citation statements)
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“…These authors also found a decrease in the total sulfhydryl group (p<0.05) (up to about 40%) as exposure time extended which was attributed to the formation of disulfide through cross-linking of sulfhydryl groups influenced by reactive species generated by cold plasma (Segat et al, 2015). Similar results were reported by Sharifian, Soltanizadeh, and Abbaszadeh (2019) who found an increase (p<0.05) in the carbonyl content of beef myofibrillar proteins after the DBD plasma treatment which was higher at increased processing times. The carbonyl formation has been attributed to the modification of certain amino acid side chains with -NH 2 or -NH, or to the cleavage of peptide bonds (Segat et al, 2015).…”
Section: Protein Oxidationsupporting
confidence: 76%
See 1 more Smart Citation
“…These authors also found a decrease in the total sulfhydryl group (p<0.05) (up to about 40%) as exposure time extended which was attributed to the formation of disulfide through cross-linking of sulfhydryl groups influenced by reactive species generated by cold plasma (Segat et al, 2015). Similar results were reported by Sharifian, Soltanizadeh, and Abbaszadeh (2019) who found an increase (p<0.05) in the carbonyl content of beef myofibrillar proteins after the DBD plasma treatment which was higher at increased processing times. The carbonyl formation has been attributed to the modification of certain amino acid side chains with -NH 2 or -NH, or to the cleavage of peptide bonds (Segat et al, 2015).…”
Section: Protein Oxidationsupporting
confidence: 76%
“…The carbonyl formation has been attributed to the modification of certain amino acid side chains with -NH 2 or -NH, or to the cleavage of peptide bonds (Segat et al, 2015). Sharifian et al (2019) reported a significant increase (p<0.05) in free sulfhydryl groups in beef myofibrillar proteins after 10 min of atmospheric cold plasma (ACP) treatment compared to the untreated samples and those treated for 5 min. According to these authors, the alteration of the terciary structure of the myofibrillar proteins caused by 10 min plasma treatment, could have facilitated the hidden sulfhydryl groups to become exposed at the protein surface and consequently, be more vulnerable to the treatment.…”
Section: Protein Oxidationmentioning
confidence: 99%
“…After DBD-CP treatment, the decrease in pH could also be related to H 2 O dissociation, thus increasing the H + concentration 27 . In addition, H 2 O 2 generated in air or liquid after treatment could lead to the formation of H 3 O + ions in PTW 2 .…”
Section: Resultsmentioning
confidence: 99%
“…Dielectric barrier discharge cold plasma (DBD-CP) is an emerging technology that has been widely applied for the functionalization and modification of proteins 1,2 , the elimination of pathogenic and spoilage microorganisms 3,4 and the curing process 5,6 of meat products. DBD-CP was used for killing microorganisms in fresh pork loin and extending the shelf life of fresh meat 7 .…”
Section: Introductionmentioning
confidence: 99%
“…Proteins comprise both hydrophilic and hydrophobic amino acid residues. The probability of hydrophilic residues appearing inside the molecule is greater than that of hydrophobic residues appearing on the surface of the molecule (Sharifian, Soltanizadeh, & Abbaszadeh, 2019). Many charged residues form salt bonds through the interaction of positive and negative charges, and some residue side chains form hydrogen bonds.…”
Section: Surface Hydrophobicitymentioning
confidence: 99%