2017
DOI: 10.1002/jsfa.8273
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Analysis of α‐helix unfolding in the pine nut peptide Lys‐Cys‐His‐Lys‐Pro induced by pulsed electric field

Abstract: PEF treatment increased peptide linkage stretch vibration and altered hydrogen bonding of KCHKP. The stability of the α-helix structure was influenced by hydrogen bonds within the peptide linkage of KCHKP induced by PEF and was related to changes in antioxidant activity. © 2017 Society of Chemical Industry.

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Cited by 22 publications
(6 citation statements)
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“…This result was in agreement with the previous research, that the β-turn structure largely disappeared and the content of the irregular structure was increased in the peanut protein hydrolysates [ 31 ]. Furthermore, a loss of α-helixes is considered to be strongly connected with the increased antioxidant activity of peptides [ 32 ]. Based on the changes of the secondary structure, it could be speculated that the polypeptide chains in DWMP were ongoing significant denaturation, and the α-helixes of the DWMP transformed into random coils after enzymatic hydrolysis.…”
Section: Resultsmentioning
confidence: 99%
“…This result was in agreement with the previous research, that the β-turn structure largely disappeared and the content of the irregular structure was increased in the peanut protein hydrolysates [ 31 ]. Furthermore, a loss of α-helixes is considered to be strongly connected with the increased antioxidant activity of peptides [ 32 ]. Based on the changes of the secondary structure, it could be speculated that the polypeptide chains in DWMP were ongoing significant denaturation, and the α-helixes of the DWMP transformed into random coils after enzymatic hydrolysis.…”
Section: Resultsmentioning
confidence: 99%
“…Under the same gradient elution program, only one peak at 220 nm with a retention time of 5.2 min was recorded, indicating that the peptide chain of QWFH was intact and not cleaved into smaller peptides following treatment with PEF. Xing et al () found that the peptide chain of Lys‐Cys‐His‐Lys‐Pro was not altered after PEF processing. Similarly, Marsellés () supported that the PEF treatment would not affect the grape juice proteins’ primary structure.…”
Section: Resultsmentioning
confidence: 99%
“…The measurement method was in accordance with the method of Xing, Zhang, Zhang, and Lin (2017). Sample concentration was 8 mg/ ml, and the flow velocity was 3.2 ml/min.…”
Section: Pef Treatmentmentioning
confidence: 99%
“…In the previous study, Yang et al has illuminated that PEF treatment promoted the antioxidant activities of pine nut peptides (KWFCT and QWFCT), which were closely related to the secondary structure of peptide solution . Xing et al found that the α-helix of the pine nut peptide KCHKP was affected by PEF . In addition, it was reported that the hydrophobic value was correlated with immunomodulatory activity, , which may enhance the interaction of peptide with cell membranes and lead to the improvement in the immune regulation .…”
Section: Introductionmentioning
confidence: 99%
“…19 Xing et al found that the α-helix of the pine nut peptide KCHKP was affected by PEF. 20 In addition, it was reported that the hydrophobic value was correlated with immunomodulatory activity, 21,22 which may enhance the interaction of peptide with cell membranes and lead to the improvement in the immune regulation. 23 In the present study, a novel peptide Alg-Gly-Ala-Val-Leu-His (RGAVLH) was extracted and purified from pine nut (P. koraiensis) protein using enzymatic Sephadex gel G-25 filtration column chromatography and high-performance liquid chromatography−tandem mass spectrometry (HPLC−MS/MS).…”
Section: ■ Introductionmentioning
confidence: 99%