In conventional fish soup processing, valuable aquatic resources like fish skins, bones, and scales are often squandered. This study was aimed at investigating if comminution combined with pressure-conduction treatment has the potential to enhance the reutilization of cooking residues. The different blending ratios of original soup (OS), made from the initial cooking of fish, and residue soup (RS), produced from processed leftover fish parts, were alternatively investigated to satisfy the new product development. Comminution combined with pressure-conduction treatment significantly increased the nutrient contents of calcium, soluble proteins and total solids in crucian carp soup (p < 0.05). With the increase in RS ratio, the decomposition of inosine monophosphate (IMP) and free amino acids was accelerated, but the accumulation of aromatic compounds was promoted simultaneously. In addition, the Maillard reaction may lead to a reduction in aldehydes, causing a diminution in the characteristic flavor of fish soup, while the formation of 1-octen-3-ol can enhance the earthiness of the fish soup. The electronic tongue test results and the sensory results showed that the blend ratio of OS and RS at 7:3 had a more significant umami and fish aroma (p < 0.05). Under this condition, the mixed soup has better nutritional values and flavor characteristics.

Aquatic products are gaining popularity due to their delicacy and high nutrient value. However, they are perishable, with a short shelf-life. Frozen storage is associated with adverse effects, leading to protein oxidation and degradation, thereby altering the protein’s structural integrity and subsequently influencing the palatability of protein-based food products. To address these challenges, novel antifreeze peptides have gained significant attention. Antifreeze peptides are a class of small molecular weight proteins or protein hydrolysates that offer protection to organisms in frozen or sub-frozen environments. They offer distinct advantages over conventional commercial antifreeze agents and natural antifreeze proteins. This review provides an overview of the current state of research on antifreeze agents, elucidates their characteristics and mechanisms, and examines their applications in aquatic products. Furthermore, the article offers insights into the prospective development and application prospects of antifreeze peptides.

The sea cucumber is an essential nutrient source and a significant economic marine resource associated with successful aquaculture. However, sea cucumbers are highly susceptible to autolysis induced by endogenous protease after postmortem, and the phenomenon of body wall “melting” occurs, which seriously affects the food quality of products and the degree of acceptance by consumers. To satisfy the growing demand for fresh or processed sea cucumbers, we must clarify the autolysis mechanism of sea cucumbers and the methods to achieve autolysis regulation. In this paper, the factors leading to the quality deterioration and texture softening of sea cucumbers are reviewed, with emphasis on enzymatic characteristics, the autolysis mechanism, the effects of autolysis on the physicochemical properties of the body wall of the sea cucumber, and the development of potential natural protease inhibitors. We aim to provide some reference in future preservation and processing processes for sea cucumbers, promote new processing and preservation technologies, and advance the sea cucumber industry’s development.

Dietary fiber is crucial in enhancing the nutritional and textural properties of surimi-based products. This study investigated blended surimi produced from silver carp and bay scallops, with the addition of different amounts (0%, 0.5%, 1%, 2%, and 3%) of inulin (INU) or psyllium husk powder (PHP) for their textural properties, protein conformation, and in vitro digestibility. The addition of INU negatively affected gel strength. However, incorporating 2.0% PHP into the blended gel improved gel strength and water-holding capacity by 8.01% and 0.79% compared to the control, respectively. Furthermore, PHP significantly increased the total sulfhydryl content and surface hydrophobicity of the blended gels (p < 0.05). Additionally, increases in endogenous fluorescence intensity accompanied by a blue shift were observed, indicating that the fluorophores (Trp and Tyr) were sequestered into a more non-polar environment due to conformational changes. The incorporation of PHP enhanced both the quality and digestibility of the blended surimi. This study provides a novel perspective for developing surimi-based food with improved quality, augmented digestion, and enhanced absorption.

Snack foods (e.g., extruded flour-based products) are widely favored by consumers because of their convenience, affordability, and time-saving attributes. However, with the growing demand for high-quality snacks, several challenges have emerged that hinder industry development, such as relatively underdeveloped industrial standards, limited raw material diversity (primarily starch and soy protein), and, consequently, insufficient nutritional value. In this study, a novel type of puffed snack was developed using Alaskan pollock surimi and wheat flour using extrusion puffing technology. The effects of varying ratios of surimi to wheat flour (0:10, 1:9, 2:8, 3:7, and 4:6, which served as SFBC, SFB1, SFB2, SFB3, and SFB4, respectively), on the physicochemical properties, apparent morphology, microstructure, thermal stability, and protein structure of spicy strips were systematically investigated, and the interaction between extruded protein and flour mixtures was analyzed. The results indicated that increasing the proportion of surimi led to decreases in hardness, elasticity, and chewiness, whereas the moisture content and water solubility index increased. The maximum expansion rate (202.2%) was observed in the SFB1 sample. Morphological and microstructural observations further revealed that a higher surimi content resulted in a denser internal structure and a reduced degree of puffing. The protein distribution was relatively uniform, with large pores. Moreover, increased surimi content increased the proportion of immobilized water and improved the thermal stability. These findings provide valuable insights into starch–protein-complex-based extrusion puffing technologies and contribute to the development of innovative surimi-based puffed food products.

The bay scallop (Argopecten irradians) adductor is an attractive raw material for the production of surimi-like products. The gelling properties of raw materials directly affect the quality of surimi-like products. To assess the potential of processing frozen bay scallop adductors into surimi-like products, the effects of short-term freezing treatment on the endogenous transglutaminase (TGase) activity, myofibrillar protein (MP) structure and gelling properties of bay scallop adductors were investigated during 14 days of frozen storage (−18 °C). The results showed that TGase activity in adductor muscles increased significantly during the first 7 days. After 7–14 days, the carbonyl and sulfhydryl contents of the MPs notably changed (increased then decreased). The β-turn content of the MPs increased, indicating stretching and flexibility. Surface hydrophobicity, fluorescence intensity and sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) analysis demonstrated changes in the tertiary structure of the MPs. Compared with gels from fresh samples, gels from scallop adductors frozen for 1 day presented significantly better texture characteristics (breaking force, gel strength, hardness, springiness, cohesiveness, chewiness) and higher water-holding capacity (p < 0.05). However, these properties significantly decreased on the 7th and 14th days (p < 0.05). Microstructural analysis revealed a more compact gel network from 1-day-frozen adductor muscles. These changes in TGase activity and MP structure are key factors influencing the gelling properties of frozen bay scallop adductors. This study provides new insights for improving gel properties during the frozen storage of bay scallop adductors.