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. 2023 Feb 9:10:1137457.
doi: 10.3389/fnut.2023.1137457. eCollection 2023.

Impact of dielectric barrier discharge cold plasma on the lipid oxidation, color stability, and protein structures of myoglobin-added washed pork muscle

Xiaoting Wang  1   2 , Jin Wang  3 , Zhaobin Wang  1 , Wenjing Yan  1 , Hong Zhuang  4 , Jianhao Zhang  1
Affiliations

Impact of dielectric barrier discharge cold plasma on the lipid oxidation, color stability, and protein structures of myoglobin-added washed pork muscle

Xiaoting Wang et al. Front Nutr. .

Abstract

Cold plasma has been considered a novel non-thermal processing technique and attracted a high attention by the food industry. In this study, the influences of dielectric barrier discharge cold plasma (DBD-CP) on the myoglobin (Mb)-added washed pork muscle (WPM) were evaluated. The electrophoresis pattern, autoxidation, and secondary structure of Mb were analyzed. The results found that DBD-CP caused the decrease of the redness and total sulfhydryl (T-SH) in WPM, while the increase of non-heme, peroxide value (PV), and thiobarbituric acid reactive substances (TBARS), suggested that treatment triggered protein oxidation and heme degradation. Additionally, DBD-CP treatment enhanced the autoxidation of Mb, induced the release of intact heme from the globin, rearranged the charged groups, and promoted Mb aggregation. The transformation of α-helix into the random coil of Mb demonstrated that DBD-CP weakened the tensile strength. Overall, data indicated that DBD-CP promoted autoxidation and changed the secondary structure of Mb, accelerating Mb-mediated lipid oxidation in WPM. Thus, further studies about the optimization of processing conditions by DBD-CP need to be performed.

Keywords: bioactive compounds; dielectric barrier discharge cold plasma; lipid oxidation; myoglobin; novel non-thermal processing technology; secondary structure.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Profiles of (A) non-heme iron contents, (B) peroxide value (PV), (C) thiobarbituric acid reactive substances (TBARS), and (D) total sulfhydryl group content (T-SH) of washed pork muscle added without and with added Mb at pH 7.0 after treatment by DBD-CP at 4°C for 4 days. Control, washed pork muscle; 0 kV, washed pork muscle added Mb; The remaining groups were treated by DBD-CP at 50, 60, 70 kV for 180 s, respectively; The operating frequency was 50 Hz. Replicates per treatment were n = 3. Means and standard deviations are shown.
Figure 2
Figure 2
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) patterns of myoglobin treated by DBD-CP at 50, 60, and 70 kV. Control, without treatment; M, molecular standards.
Figure 3
Figure 3
(A) The UV absorption. (B) metMb proportion and autoxidation rate (kox), (C) particle size distribution, and (D) zeta potential of myoglobin with and without DBD-CP treatment. koxis equivalent to the probability of decay of a single molecule to the ferric form in 4 days. Note: Control, protein without DBD-CP treatment; The remaining groups were treated by DBD-CP at 50, 60, 70 kV, and 50 Hz for 180 s, respectively. The operating frequency was 50 Hz. Replicates per treatment were n = 3. Means and standard deviations are shown.
Figure 4
Figure 4
Effect of DBD-CP on the secondary structure of myoglobin. (A) Circular dichroism (CD) spectra of Mb treated by different voltage. (B) The secondary structural changes of myoglobin were calculated from CD spectra; each sample was analyzed in triplicate; different small letters indicate significant differences (p < 0.05).
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