Although freezing has been used to delay the deterioration of product quality and extend its shelf life, the formation of ice crystals inevitably destroys product quality. This comprehensive review describes detailed information on the effects of ice crystals on aquatic products during freezing storage. The affecting factors (including nucleation temperature, freezing point, freezing rate, and temperature fluctuation) on the size, number, distribution, and shape of ice crystals are also elaborated in detail. Meanwhile, the corresponding technologies to control ice crystals have been developed based on these affecting factors to control the formation of ice crystals by inhibiting or inducing ice crystallization. In addition, the effects of ice crystals on the water, texture, and protein of aquatic products are comprehensively discussed, and the paper tries to describe their underlying mechanisms. This review can provide an understanding of ice crystallization in the aquatic products during freezing and contribute more clues for maintaining frozen food quality.

This study aimed to explore the effect of dehydration on the water migrating property and protein changes of large yellow croaker during frozen storage. A freeze-dryer was used to accelerate experiments, which was isolated from oxygen and excluded the effects of protein oxidation. After dehydration time (3, 9, 18, and 30 h) for both fast- and slow-freezing samples, the results showed that the ice sublimation of samples containing small ice crystals was faster than that of samples containing large ice crystals in the early stages of dehydration, but in the latest stage, there was an opposite trend. The results indicated that dehydration reduced the water freedom degrees and water–protein interaction. At the same time, dehydration had a significant effect on protein secondary and tertiary structures. The significant increase in surface hydrophobicity and particle size indicated that dehydration exacerbated myofibrillar protein aggregation. The ΔH1 values (from 1.275 to 0.834 J/g for slow-freezing group and from 1.129 to 0.855 J/g for fast-freezing group) decreased gradually as the dehydration time extended, indicating the decrease in protein thermal stability. Additionally, significant protein degradation occurred when the water content of the sample decreased to a certain level. This study showed that ice crystal size had an important effect on the rate of ice sublimation, and the occurrence of dehydration during frozen storage accelerated the water loss and the decrease in protein stability.

To prepare dual-functional seasoning ingredients with a salty-umami taste, five proteases were applied to hydrolyze Monetaria moneta proteins, preparing enzymatic hydrolysates. Their taste compounds along with the salty-umami taste, were investigated. The results revealed that enzymatic hydrolysis facilitated the release of taste compounds from M. moneta. The whiteness and < 3 kDa peptides of enzymatic hydrolysates significantly increased. Moreover, flavorzyme and protamex, with high DHs, could thoroughly hydrolyze the proteins, generating the enzymatic hydrolysates abundant in taste compounds (e.g., amino acids, nucleotides) that synergistically provided a strong salty-umami taste. Saltiness and umami posed a strong positive correlation, with a correlation coefficient exceeding 0.90, resulting in the highest levels of equivalent salty intensity (ESI = 80.05 gNaCl/L) and equivalent umami concentration (EUC = 84.56 gMSG/100 g) in the flavorzyme-treated hydrolysate, followed by the protamex-treated hydrolysate. In summary, these findings offer novel insights into preparing dual-functional seasoning ingredients with a salty-umami taste, ideal for use in low-salt food production.