Jing Lu

Mussels are nutrient-rich but perishable, resulting in substantial resource loss. A protease-producing strain (Bacillus velezensis Z-1, Mytilus edulis) isolated from marine sludge was used to hydrolyze mussels, producing Y-1, a hydrolysate with antioxidant activity. In this study, ultrafiltration, gel chromatography, and LC-MS/MS were employed to isolate and identify bioactive peptides from the hydrolysate. The results revealed that the hydrolysate exhibited antioxidant activity, pancreatic cholesterol esterase inhibitory activity, pancreatic lipase inhibitory activity, and α-glucosidase inhibitory activity. Molecular docking using AutoDock Tools 1.5.6 was performed to analyze the interactions of peptides with CD38 and Keap1, leading to the identification of five potentially bioactive peptides: VPPFY, IMLFP, LPFLF, FLPF, and FPRIM. These peptides formed hydrogen bonds and hydrophobic interactions with CD38 and Keap1, demonstrating strong DPPH radical scavenging and superoxide anion radical scavenging capacities. This study highlights the multifunctional bioactive potential of these peptides, offering insights into their therapeutic applications. The findings provide a novel approach for the effective utilization of mussel resources and highlight their potential application value in the development of functional foods.

The alkaline protease from Bacillus licheniformis strain 2709 (AprE 2709) is widely used in Chinese industries but faces stability challenges under high-temperature conditions. This study employed molecular modeling and mutagenesis to identify Asn residues at positions 61, 160, and 211 as key sites affecting the stability of AprE 2709. By leveraging the additive and cooperative effects of mutations, the mutant enzyme AprE 2709 (N61G/N160G/N211G) was engineered, exhibiting enhanced thermostability and catalytic activity. The mutant demonstrated a 2.89-fold increase in half-life at 60 °C and a 1.56-fold improvement in catalytic efficiency compared to the wild-type enzyme. Structural analysis revealed that the improved thermostability was due to altered electrostatic interactions and strengthened hydrophobic contacts. Targeting Asn residues prone to deamidation presents a promising strategy for improving protein heat tolerance. These findings not only enhance our understanding of enzyme stability but also lay a foundation for future research aimed at optimizing alkaline proteases for diverse industrial applications, particularly in high-temperature processes.

Biological denitrification is an efficient and low-cost method to treat wastewater, and it has been shown that growth promoters can regulate the metabolism of microorganisms. This study aimed to investigate the effects of gibberellic acid, naphthalene acetic acid, compound sodium nitrophenolate, and diethyl aminoethyl hexanoate on the growth and denitrification process of denitrifying microorganisms and to examine the associated mechanisms. All four tested growth promoters did not affect the growth of the strain Q1; further, compound sodium nitrophenolate could significantly improve the bacterial denitrification efficiency and showed an increase in the removal rate of 13.08% in 72 h. The addition of 15 mg/L compound sodium nitrophenolate increased the removal rate of strain Q1 by 25.88% at 72 h, significantly improving the efficiency of reducing the chemical oxygen demand of the effluent. Transcriptome analysis identified 1664 differentially expressed genes (573 upregulated and 1091 downregulated genes) in the strain Q1 treated with compound sodium nitrophenolate. Nitrate reductase and nitrate transporter, which are two key enzymes related to the nitrate reduction pathway, were found to be upregulated during the denitrification process. Compound sodium nitrophenolate has promising applications in high-salt and high-nitrogen wastewater treatment.