Abstract
Frozen surimi sol incline to protein oxidation, but the quality control strategies based on oxidation remain limited. Hence, the antioxidant and cryoprotective effects of γ-polyglutamic acid (γ-PGA) on freeze-thawed salt-dissolved myofibrillar protein (MP) sol were investigated. Results showed that γ-PGA could effectively regulate protein oxidation of MP sol during freeze-thawing with lower carbonyl contents and less oxidative cross-linking. Meanwhile, γ-PGA primely maintained sol protein structures, showing reduction of 15.28% of salt soluble protein contents at γ-PGA addition of 0.04% under unoxidized condition. Additionally, compared to the control group without oxidation treatment, cooking loss of heat-induced gel with 0.04% γ-PGA decreased by 47.19%, while gel strength obviously increased by 57.22% respectively. Overall, moderate γ-PGA addition (0.04%) could inhibit protein oxidation of sol, further improving frozen stability of sol through hydrogen bonds and hydrophobic interaction, but excessive γ-PGA was adverse to sol quality due to severe cross-linking between γ-PGA and MP.
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