Abstract

Tracking aggregation behaviour and changes in emulsifying properties of myofibrillar protein from mirror carp (Cyprinus carpio L.) induced by its oxidation during frozen storage under the effect of ice structuring protein were investigated. Solubility, net charge, emulsion properties of the sample without ice structuring protein decreased, meanwhile carbonyl, turbidity, the mean diameter in volume and the mean diameter in surface increased during frozen storage. As ice structuring protein addition increased, water-holding capacity and emulsifying properties of samples showed a trend of first increasing and then decreasing, while the tendency of oxidation and aggregation was opposite. Ice structuring protein of 2.0 (g/L) caused the most significant results (P < 0.05). Carbonyl, solubility and emulsion activity index of samples with 2.0 g/L ice structuring protein were decreased by 10.0%, 14.3% and 34.6% after 180 d, respectively. Results suggested that ice structuring protein could effectively prevent moisture loss from flesh, inhibit myofibrillar protein oxidation, and improve emulsion stability during frozen storage.

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 call

Disclaimer: 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.