Excellent quality acquisition of myofibrillar protein in red shrimp (Solenocera crassicornis) based on regulating the oxidation degree of atmospheric cold plasma treatment.

Abstract

Background: Myofibrillar protein (MP) is essential for the texture and taste of shrimp surimi products. The reactive oxygen/nitrogen species (ROS/RNS) produced by atmospheric cold plasma (ACP) might cause oxidative modification of MP. In this study, the effect of different ACP treatment times on the properties of red shrimp MP was investigated in detail.

Results: The mild oxidation induced by ACP treatment for 1 min (ACP-1 min) promoted the unfolding and refolding of the MP structure, which was manifested as a transition from α-helix to β-sheets. Compared with other groups, more hydrogen bonds and hydrophobic interactions in the ACP-1 min group might enhance the interactions between the myosin heavy chain and actin, which was conducive to the formation of a regular and dense three-dimensional network structure. Person correlation analysis revealed that ROS/RNS mediated the changes in the secondary and tertiary structure of MP. In addition, ACP-1 min has high Ca²⁺-ATPase activity, which reflected that MP maintained structural integrity. While excessive oxidation in the ACP treatments for 3 min and 5 min reduced MP robustness. The stable internal structure in ACP-1 min group gave the MP excellent texture profile (1.79 mJ of adhesiveness and 0.89 mm of springiness) and rheological characteristics (0.373 MPa of storage modulus).

Conclusion: Overall, the excellent quality of MP could be obtained by regulating the oxidation degree of ACP, which would provide valuable information for the in-depth and efficient processing of shrimp products. © 2024 Society of Chemical Industry.