Abstract
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 effect 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 α-helix and β-sheet proportion. Finally, the ABTS ((2,2′-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.
Highlights
In recent years, ultrasonic pulses have been used as an environmentally-friendly technology to improve the functional properties of vegetable and animal proteins by altering their hydrogen bonds and hydrophobic interactions, as well as by disrupting their molecular conformation through cavitation, heating, dynamic agitation and shear stress [1]
The treatments are identified as Ultrasound-pulsed gelatins (UPG)-42, UPG-52, UPG-71, and UPG-84, respectively, and control gelatin (CG)
The gelatins in this study showed antioxidant activity in the range of
Summary
Ultrasonic pulses have been used as an environmentally-friendly technology to improve the functional properties of vegetable and animal proteins by altering their hydrogen bonds and hydrophobic interactions, as well as by disrupting their molecular conformation through cavitation, heating, dynamic agitation and shear stress [1]. This technology has been used in green chemistry as a tool for the extraction of functional compounds with an improved yield, short time, low cost, and less solvent [2].
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
