%0 Journal Article
%T 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.
%A Yan S
%A Du Z
%A Liu C
%A Yu D
%A Zhu Z
%A Xu J
%A Xia W
%A Xu Y
%J Food Chem
%V 451
%N 0
%D 2024 Sep 1
%M 38670022
%F 9.231
%R 10.1016/j.foodchem.2024.139456
%X 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.