Abstract

This study was done to analyze the cryoprotective influence of ovalbumin (OVA) with kappa-carrageenan (KC) in grass carp myofibrillar proteins during frozen storage. Ca2+-ATPase activity of MP was significantly reduced due to protein denaturation and showed a direct association with decreased sulphydryl (SH) contents and tertiary structural properties. Besides that, an increase in carbonyl, surface hydrophobicity, and dityrosine contents was observed. The addition of OVA-KC significantly restricted the decline in Ca2+-ATPase and SH groups, which were further confirmed by the retarded increase in carbonyls. Furthermore, the addition of OVA-KC increased the stability of α-helix contents. Moreover, MP treated with 6% OVA-KC also improved intermolecular interaction forces linked with gelling and water holding properties of MP. Therefore, it can be concluded that OVA-KC could be used as an effective cryoprotectant in fish and related products for preservation and commercialization.

Highlights

  • Grass carp (Ctenopharyngodon idella) is one of the major freshwater fish species in China due to its low prices, better yield, and growth [1]

  • The current study proposes the addition of OVA-KC as an effective approach to prevent the formation of carbonyls due to their proper cross-linking with amino acid molecules, which can reduce protein–water and protein–protein interactions during frozen storage

  • At the beginning of storage, no significant reduced the rate of oxidation in muscle proteins by binding at the func differences were observed between control and MP treated with different concentrations sites of proteins though proper cross-linking and prevented the freeze-induced ch of OVA-KC

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Summary

Introduction

Grass carp (Ctenopharyngodon idella) is one of the major freshwater fish species in China due to its low prices, better yield, and growth [1]. Oxidative modifications are primarily responsible for the decrease in flavor, gelling, and textural characteristics of final product These changes are driven by MP oxidation and alteration in intermolecular covalent interaction forces [7]. OVA can be used as an efficient emulsifier and gelling agent, which can act as an enzyme inhibitor to prevent the functional losses in surimi products [17] In this regard, OVA has been reported as an effective antioxidative agent due to the presence of sulfhydryl groups and strong binding abilities with metal ions. This study deals with the functional, conformational, and intermolecular interaction forces between the MP and OVAKC, especially focusing on the potential antioxidant properties It sheds light on the application of OVA-KC as an effective additive and as a low sweetness cryoprotectants in the prolonged commercialization of fish and related products during frozen storage

Materials
Extraction of Myofibrillar Proteins
Preparation of Samples
Determination of Protein Solubility
Determination of Carbonyl Content
Determination of Sulfhydryl Content
Determination of Dityrosine Content
2.10. Surface Hydrophobicity
2.13. Intermolecular Interaction Force
2.14. Statistical Analysis
Protein Solubility
Carbonyl Content
Sulfhydryl Content
Dityrosine Content
Circular Dichroism
Intermolecular Interaction Force
Conclusions
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