Journal
APPLIED SCIENCES-BASEL
Volume 10, Issue 3, Pages -Publisher
MDPI
DOI: 10.3390/app10031004
Keywords
high-intensity ultrasound pulses; gelatin; antioxidant; unfolding
Categories
Funding
- CONACyT
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Ultrasonic pulses are considered green technology for the improvement of the functional properties of proteins. In this study, four high-intensity ultrasound pulse treatments (ultrasound-pulsed gelatin (UPG)-42, UPG-52, UPG-71, UPG-84, and non-pulsed control gelatin (CG)) were applied to tilapia (Oreochromis niloticus) skin gelatin in order to study their e ffect on its physicochemical and antioxidant properties; a non-treated gelatin was used as a control. UPGs showed a significant increase in soluble protein and surface hydrophobicity compared to the control gelatin, and no significant difference was found in the electrophoretic profiles. The effects on the secondary structure were studied by circular dichroism and infrared spectra, and these showed that the random coil conformation was the main component in all treatments and the ultrasonic treatments only affected the ff-helix and fi-sheet proportion. Finally, the ABTS ((2,20-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)) and FRAP (ferric reducing ability) assays demonstrated that ultrasound treatments could improve the antioxidant activity of gelatins as free radical scavengers and electron donors. These results suggest that high-intensity ultrasound pulse technology is useful to improve fish gelatin antioxidant properties, which could be associated with secondary structure disruption.
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