Combined ATAC-seq, RNA-seq, and GWAS analysis reveals glycogen metabolism regulatory network in Jinjiang oyster ( Crassostrea ariakensis).

Glycogen serves as the principal energy reserve for metabolic processes in aquatic shellfish and substantially contributes to the flavor and quality of oysters. The Jinjiang oyster ( Crassostrea ariakensis) is an economically and ecologically important species in China. In the present study, RNA sequencing (RNA-seq) and assay for transposase-accessible chromatin using sequencing (ATAC-seq) were performed to investigate gene expression and chromatin accessibility variations in oysters with different glycogen contents. Analysis identified 9 483 differentially expressed genes (DEGs) and 7 215 genes with significantly differential chromatin accessibility (DCAGs) were obtained, with an overlap of 2 600 genes between them. Notably, a significant proportion of these genes were enriched in pathways related to glycogen metabolism, including "Glycogen metabolic process" and "Starch and sucrose metabolism". In addition, genome-wide association study (GWAS) identified 526 single nucleotide polymorphism (SNP) loci associated with glycogen content. These loci corresponded to 241 genes, 63 of which were categorized as both DEGs and DCAGs. This study enriches basic research data and provides insights into the molecular mechanisms underlying the regulation of glycogen metabolism in C. ariakensis.

Cross-linked tyrosinase aggregates for elimination of phenolic compounds from wastewater.

A novel, practical and inexpensive immobilization method has been developed for mushroom tyrosinase to be used for enzymatic treatment of phenolic wastewater. Catalyzed by the enzyme immobilized in the form of cross-linked enzyme aggregates (CLEAs), phenolic compounds such as phenol, p-cresol, p-chlorophenol and bisphenol A can be efficiently eliminated, with a complete conversion obtained within 0.5-3h, superior to other processes catalyzed by the same enzyme which is either free or immobilized with traditional carrier-bound immobilization methods. The effects of reaction time, pH, enzyme dosage and initial concentration of the phenol solution were examined. The sequence of dephenolization rate (p-cresol>p-chlorophenol>phenol) was in accordance with the substrate selectivity of the enzyme. The reusability of the CLEAs has been tested in a batch reactor for each phenol. In a continuous stirred tank reactor, the CLEAs encapsulated into calcium alginate gels were effective for removing phenol for at least 26h. The toxicity of the phenol-containing solution was remarkably diminished after treatment with the tyrosinase CLEAs, as demonstrated by the Hydra sinensis test.

Activity and stability of cross-linked tyrosinase aggregates in aqueous and nonaqueous media.

Cross-linked tyrosinase aggregates were prepared by precipitating the enzyme with ammonium sulfate and subsequent cross-linking with glutaraldehyde. Both activity and stability of these cross-linked enzyme aggregates (CLEAs) in aqueous solution, organic solvents, and ionic liquids have been investigated. Immobilization effectively improved the stability of the enzyme in aqueous solution against various deactivating conditions such as pH, temperature, denaturants, inhibitors, and organic solvents. The stability of the CLEAs in various organic solvents such as tert-butanol (t(1/2)=326.7h at 40°C) was significantly enhanced relative to that in aqueous solution (t(1/2)=5.5h). The effect of thermodynamic water activity (a(w)) on the CLEA activity in organic media was examined, demonstrating that the enzyme incorporated into CLEAs required an extensive hydration (with an a(w) approaching 1.0) for optimizing its activity. The impact of ionic liquids on the CLEA activity in aqueous solution was also assessed.