Protein oxidation/aggregation during ultrasound thawing at different powers impair the gel properties of common carp (Cyprinus carpio) myofibrillar protein

Abstract

The influences of ultrasound thawing (UT) at different power (0, 100, 300, and 500 W) on the oxidation, aggregation, and gel properties of common carp (Cyprinus carpio) myofibrillar protein were evaluated in the present study. The free amino content, carbonyl content, dityrosine content, and TBARS value of UT-300 were significantly lower than those of other thawing groups (P < 0.05), suggesting that appropriate ultrasound power (300 W) thawing inhibited the oxidation of myofibrillar protein and fat. However, excessive power (500 W) UT enhanced the oxidation of fish protein. UT-300 had the smallest surface hydrophobicity, particle size, and turbidity values, indicating that UT-300 reduced protein aggregation caused by thawing. At the same time, UT-300 protein gel had a higher gel strength and water-holding capacity than other thawing treatments, which were characterized by fine and uniform gel networks. Water distribution analysis also proved that UT-300 inhibited the loss of bound water, free water, and immobilized water, as well as the increase in fluidity caused by thawing. In conclusion, proper power (300 W) UT was beneficial in inhibiting the degradation of gel properties caused by protein oxidation and aggregation during thawing.