Uncovering quality changes of surimi-sol based products subjected to freeze–thaw process: The potential role of oxidative modification on salt-dissolved myofibrillar protein aggregation and gelling properties

Abstract

Frozen surimi quality generally correlates with oxidation, but impacts of protein oxidation on salt-dissolved myofibrillar protein (MP) sol in surimi remain unclear. Hence, physicochemical and gelling properties of MP sol with different oxidation degrees were investigated subjected to freeze–thaw cycles. Results showed that mild oxidation (≤1 mmol/L) improved unfrozen MP gel quality with lowest cooking loss (3.29 %) and highest hardness (829.76 N). Whereas, oxidized sol suffering freeze-thawing degenerated severely, showing reduction of 23.85 % of salt soluble protein contents with H2O2 concentrations of 10 mmol/L. Shearing before heating influenced gelling properties of freeze-thawed sol, depending on oxidation levels. Oxidized gel with shearing displayed disorganized network structures, whereas gel without shearing displayed relatively complete appearances without holes under high oxidation condition (10 mmol/L). Overall, freeze–thaw process aggravated denaturation extents of MP sol subjected to oxidation, further causing high water loss and yellow color of heat-induced gel, especially to gel with shearing.