BACKGROUND: Quite recently, considerable attention has been paid to atmospheric cold plasma (ACP) as an eco-friendly and highly efficient technology to modify the functional properties of foods. This study focuses on the effect of ACP on the myofibril protein and lipid quality of hairtail (Trichiurus lepturus) fish. In achieving this, the samples were treated with ACP at 50 kV for different times (30, 60, 120, 180, 240, 300 s).
RESULTS:The findings indicated slight changes in peroxide value and thiobarbituric acid reactive substances in the samples treated with ACP. A significant increase (P < 0.05) in the surface hydrophobicity (from 131.71 ± 0.81 ∼g to 146. 34 ± 0.81 ∼g), turbidity (from 0.13 ± 0.001 to 0.27 ± 0.01), and water-holding capacity (from 61.63% ± 5.7% to 64.86% ± 1.5%) were detected with treated samples. CONCLUSIONS: We conclude that ACP treatment induces marked changes in the protein and lipid properties of myofibril protein isolated from hairtail fish, which strengthen the gel formation of hairtail fish.
The changes in the functional properties of trypsin from shrimps (Litopenaeus vannamei) after, Atmospheric Cold Plasma (ACP) treatments, have been evaluated in terms of enzyme inactivation, surface hydrophobicity, secondary structure, fluorescence intensity, and particle size distribution. Different exposure voltages of 10, 20, 30, 40, and 50 kV at various treatment times (1, 2, 3, and 4 min) have been employed, in a separate assay. The results showed that trypsin-like protease activity decreased (by about 50%), and the kinetic constants Km value increased, while the kcat value decreased. Surface hydrophobicity and fluorescence intensity revealed a significant increase compared to the control sample. A high degree of protein degradation has been noticed by SDS-PAGE analysis. In addition, circular dichroism indicated that random coil and α-helix contents declined while β-turn and β-sheet contents have raised. A sharp drop in the particle size was observed with increasing the treatment voltage from 0 to 40 kV for 4 min, and the corresponding peak reached the minimum of 531.2 nm. Summing up the results, it can be concluded that the ACP technique effectively affects the activity of trypsin-like protease, which in terms enhances the quality of dietary protein.
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