Work

Mechanisms of quality deterioration in noodle-shaped surimi gels: Insights from the impact of setting temperatures on protein structure

Year: 2025

Type: article

Abstract: Background: Quality deterioration in noodle-shaped surimi gels (NS) occurred when setting temperatures exceed 35°C, yet the underlying structural mechanisms remain unclear. This study investigated the effects of setting temperatures on protein structural transitions and NS quality. Method: Rheological behavior, molecular chain integrity, protein conformation, and endogenous enzymatic activity were systematically evaluated under different setting temperatures. Results: NS exhibited optimal gelling performance between 30 and 35°C, while rigidity, elasticity, and molding capability declined sharply at 40°C. During the chopping and setting, elevated temperatures led to a loss of hydrogen bonds and Ca²⁺-ATPase activity, while hydrophobic interactions intensified. A critical threshold at 35°C induced α-helix-to-β-sheet transitions and promoted excessive protein aggregation. Consequently, molecular chain integrity and viscoelastic properties were markedly compromised above 35°C. Conclusions: Quality deterioration of NS above 35°C is attributed to dual mechanisms: (1) the broken hydrogen bonds in fish pastes drive the transformation from α-helical to β-folded structure; (2) the hydrophobic groups of NS being buried by the protein aggregates, weakening its molecular chain and rheological properties. These findings elucidated the protein structural basis of NS quality deterioration and provide theoretical guidance for optimizing NS processing.

Source: LWT

DOI: 10.1016/j.lwt.2025.118946