Gelation Properties of Surimi Protein Systems

Surimi is a refined fish-protein concentrate widely used to produce a variety of seafood analogue products. Gelation in surimi systems arises when myofibrillar proteins, predominantly myosin and actin, unfold upon heating and subsequently reaggregate to form a three-dimensional network that entraps water, fat and small molecules. The resulting gel matrix determines key textural attributes such as firmness, elasticity and water-holding capacity, which are critical for consumer acceptability and industrial performance. Gel quality is influenced by factors including protein conformation, ionic strength, heating regime (setting or direct heating), endogenous enzymes and the inclusion of polysaccharides or other functional additives. Advances in spectroscopic, rheological and microscopic methods have deepened understanding of the molecular transitions, network architecture and interfacial phenomena that underlie surimi gel formation, enabling targeted modulation of texture, stability and nutritional profile for applications ranging from fish balls to plant-based analogues.

Research from Nature Portfolio

Recent studies have employed advanced spectroscopic and microscopic techniques to elucidate the molecular transformations that underpin gel formation in white croaker surimi. Analysis of amide I band profiles during progressive heating has revealed partial conversion of α-helical regions of myosin into β-sheet, β-turn and random coil motifs. β-sheets and random coils appear crucial to the stability of the three-dimensional protein network, with β-sheet content correlating strongly with measured gel strength. Scanning electron microscopy further demonstrated that higher-grade surimi gels exhibit more ordered, fibrous networks, accounting for improved textural properties. These findings underscore the importance of secondary-structure transitions in controlling gel quality and offer a quantitative framework for predicting functional performance.

Gelation Properties of Surimi Protein Systems publication trend

The graph below shows the total number of articles in gelation properties of surimi protein systems across all publications each year (not limited to Nature Index journals).

Technical terms

Surimi: A concentrated myofibrillar protein paste prepared from washed and refined fish mince, used as a precursor for seafood analogue products.

Gelation: The process by which solubilised proteins undergo heat-induced unfolding and reaggregation to form a three-dimensional network that traps water and fat.

Myofibrillar proteins: The salt-soluble muscle proteins, primarily myosin and actin, responsible for the gel-forming ability of surimi.

β-sheet: A secondary-structure motif formed by hydrogen bonding between adjacent polypeptide strands, contributing to gel network strength.

Storage modulus (Gʹ): A rheological parameter reflecting the elastic component of a gel under oscillatory deformation, indicative of network firmness.

References

1. Analysis of protein structure changes and quality regulation of surimi during gelation based on infrared spectroscopy and microscopic imaging. Scientific Reports (2018).
2. Effect of Psyllium (Plantago ovata Forks) Husk on Characteristics, Rheological and Textural Properties of Threadfin Bream Surimi Gel. Foods (2021).
3. Effects of curdlan on the texture and structure of Alaska pollock surimi gels treated at 120°C. International Journal of Food Properties (2018).
4. Insight into the Gel Properties of Antarctic Krill and Pacific White Shrimp Surimi Gels and the Feasibility of Polysaccharides as Texture Enhancers of Antarctic Krill Surimi Gels. Foods (2022).