Cipangopaludina cathayensis (Gastropoda: Prosobranchia; Mesogastropoda; Viviparidae) is widely distributed in the freshwater habitats of China. It is an economically important snail with high edible and medicinal value. However, the genomic resources and the reference genome of this snail are lacking. In this study, we assembled the first chromosome-level genome of C. cathayensis. The preliminary assembly genome was 1.48 Gb in size, with a contig N50 size of 93.49 Mb. The assembled sequences were anchored to nine pseudochromosomes using Hi-C data. The final genome after Hi-C correction was 1.48 Gb, with a contig N50 of 98.49 Mb and scaffold N50 of 195.21 Mb. The anchored rate of the chromosome was 99.99%. A total of 22,702 protein-coding genes were predicted. Phylogenetic analyses indicated that C. cathayensis diverged with Bellamya purificata approximately 158.10 million years ago. There were 268 expanded and 505 contracted gene families in C. cathayensis when compared with its most recent common ancestor. Five putative genes under positive selection in C. cathayensis were identified (false discovery rate <0.05). These genome data provide a valuable resource for evolutionary studies of the family Viviparidae, and for the genetic improvement of C. cathayensis.

Solenaia oleivora, a rare freshwater shellfish with high protein quality, is unique to China. However, the poor hydrosolubility and functional properties of Solenaia oleivora proteins hinder their utilization in food products. Herein, the alkaline dissolution-isoelectric precipitation method was used for the extraction of Solenaia oleivora proteins. Furthermore, the impact of high-pressure homogenization (HPH) treatment varying from 0 to 100 MPa on the structure and functional properties of Solenaia oleivora proteins was investigated. The obtained results indicated that HPH treatment decreased the α-helix content and enhanced the β-sheet and random coil content. Furthermore, the HPH caused the unfolding of protein structure, exposing aromatic amino acids, increasing the free thiol group content, and enhancing surface hydrophobicity. As the homogenization pressure increased from 0 to 100 MPa, the particle size of Solenaia oleivora proteins decreased from 899 to 197 nm with the polymer dispersity index (PDI) value decreased from 0.418 to 0.151, the ζ-potential increased from −22.82 to −43.26 mV, and the solubility increased from 9.54% to 89.96%. Owing to the significant changes in protein structure and solubility, the emulsifying, foaming, and digestive properties of Solenaia oleivora proteins have been significantly improved after treatment with HPH.

Protein-based emulsion gels are an ideal delivery system due to their unique structure, remarkable encapsulation efficiency, and tunable digestive behavior. Freshwater mussel (Solenaia oleivora) protein isolate (SoPI), an emerging sustainable protein with high nutritional value, possesses unique value in the development of functional foods. Herein, composite emulsion gels were fabricated with SoPI and κ-carrageenan (κ-CG) for the delivery of curcumin. SoPI/κ-CG stabilized emulsions possessed a high encapsulation efficiency of curcumin with a value of around 95%. The addition of κ-CG above 0.50% facilitated the emulsion gel formation and significantly improved the gel strength with 1326 g. Furthermore, the storage and digestive stability of curcumin were significantly improved as the κ-CG concentration increased. At 1.50% κ-CG, around 80% and 90% curcumin remained after 21-day storage at 45 °C and the 6 h in vitro gastrointestinal digestion, respectively. The addition of 0.50% κ-CG obtained the highest bioaccessibility of curcumin (~60%). This study illustrated the potential of SoPI emulsion gels as a carrier for stabilizing and delivering hydrophobic polyphenols.

Variations in salinity levels in aquaculture significantly influence fish physiology, impacting population dynamics and industry viability. This study aimed to examine the physiological response of the freshwater drum (Aplodinotus grunniens) to differing salinity conditions, assessing its potential for cultivation in brackish water environments. Fish averaging 45 ± 0.1 g were subjected to acute salinity tests across three groups: a control group at 0‰ and experimental groups at 7.5‰ and 15‰ over four days. The initial findings indicated that A. grunniens could tolerate salinity levels up to 15‰ without adverse effects. Key biochemical markers, such as aspartate aminotransferase and alanine aminotransferase, exhibited significant fluctuations but decreased over time. Antioxidant enzyme activity increased relative to the control, while malondialdehyde levels declined, indicating effective oxidative stress management. Additionally, digestive enzymes like amylase and lipase demonstrated adaptability to changing salinity. The expression of heat shock proteins 70 and 90 in the gills and livers varied initially but showed no sustained changes. Overall, the results suggest that A. grunniens possesses notable resilience to salinity variations, indicating its suitability for brackish water aquaculture and highlighting the optimal salinity ranges for promoting growth.

Salinity is a significant environmental component that affects the physiological state of aquatic species. This study aimed to investigate whether water salinity had an impact on the biochemical properties and meat quality of adult Aplodinotus grunniens during temporary rearing of 7 days. Salinity caused increased osmotic pressure and antioxidant enzyme activities of Aplodinotus grunniens, which were attributed to the increase in the content of alanine and glutamate. It raised the hardness and shear force with an increase in salinity, leading to an increase in water-holding capacity. Salinity enhanced the DHA ratio with a decrease in the atherosclerotic index and thrombosis index. Combined with the increase in flavor amino acids and nucleotides, salinity enhanced the umami taste of Aplodinotus grunniens. These findings suggest that temporary rearing in salinity might be a practical approach to improving the meat quality of adult Aplodinotus grunniens.