Qin Hu
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Qin Hu has a total of 23 co-authors. Here are the top co-authors by number of shared publications:
- Anand Kumar
Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Key Laboratory of Advanced Processing of Aquatic Product of Guangdong Higher Education Institution, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China
1 shared publication - Chaowan Guo
Guangdong Marubi Biotechnology Co., Ltd., Guangzhou 510700, China
1 shared publication - Chen Wang
Southern Marine Science and Engineering Guangdong Laboratory (Zhanjiang), Zhanjiang 524006, China
1 shared publication - Chunhua Zhu
Fisheries College, Guangdong Ocean University, Zhanjiang 524088, China
1 shared publication - Dongying Zhang
Development and Research Center for Biological Marine Resources, Southern Marine Science and Engineering Guangdong Laboratory (Zhanjiang), Zhanjiang 524025, China
1 shared publication - Hang Li
Development and Research Center for Biological Marine Resources, Southern Marine Science and Engineering Guangdong Laboratory (Zhanjiang), Zhanjiang 524025, China
1 shared publication
Latest Publications
- Open Access
Transcriptome Analyses Reveal the Molecular Response of Juvenile Greater Amberjack (Seriola dumerili) to Marine Heatwaves
Marine heatwaves (MHWs) have recently become more frequent, intense, and prolonged, posing significant threats to marine life and fisheries. In this study, transcriptomic analysis was employed to investigate the genes and pathways in Seriola dumerili that respond to MHW-induced stress at 28 °C (T28) and 32 °C (T32), using 24 °C (T24) as the control. Transcriptome sequencing revealed that 17 differentially expressed genes (DEGs) belonging to the heat shock protein (HSP) families—HSP30, HSP40, HSP70, and HSP90—were significantly upregulated under short-lasting MHW stress in the T24-4d vs. T32-4d comparison. Additionally, genes related to oxidative stress (e.g., protein disulfide isomerase family A member 6 [pdia6]), immune responses (e.g., interferon regulatory factor 5 [irf5]), and energy metabolism (e.g., hexokinase-1 [hk1]) were also identified. Enrichment analysis of DEGs in the T24-4d vs. T32-4d group revealed that S. dumerili exhibited adaptive responses to MHWs through the upregulation of HSPs and the activation of antioxidant, energy metabolism, and immune response pathways. However, in the T24-13d vs. T32-13d group, DEGs associated with these pathways were either not significantly expressed or were downregulated. These findings indicate that S. dumerili is unable to sustain its adaptive responses under repeated, intense MHW exposure, resulting in the disorder of its antioxidant defense system, immune suppression, and metabolic dysfunction. This study provides valuable insights into the molecular responses of S. dumerili to MHWs and supports the selection for thermal resistance in this species.
Open AccessTranscriptome Analyses Reveal the Molecular Response of Juvenile Greater Amberjack (Seriola dumerili) to Marine Heatwaves
Marine heatwaves (MHWs) have recently become more frequent, intense, and prolonged, posing significant threats to marine life and fisheries. In this study, transcriptomic analysis was employed to investigate the genes and pathways in Seriola dumerili that respond to MHW-induced stress at 28 °C (T28) and 32 °C (T32), using 24 °C (T24) as the control. Transcriptome sequencing revealed that 17 differentially expressed genes (DEGs) belonging to the heat shock protein (HSP) families—HSP30, HSP40, HSP70, and HSP90—were significantly upregulated under short-lasting MHW stress in the T24-4d vs. T32-4d comparison. Additionally, genes related to oxidative stress (e.g., protein disulfide isomerase family A member 6 [pdia6]), immune responses (e.g., interferon regulatory factor 5 [irf5]), and energy metabolism (e.g., hexokinase-1 [hk1]) were also identified. Enrichment analysis of DEGs in the T24-4d vs. T32-4d group revealed that S. dumerili exhibited adaptive responses to MHWs through the upregulation of HSPs and the activation of antioxidant, energy metabolism, and immune response pathways. However, in the T24-13d vs. T32-13d group, DEGs associated with these pathways were either not significantly expressed or were downregulated. These findings indicate that S. dumerili is unable to sustain its adaptive responses under repeated, intense MHW exposure, resulting in the disorder of its antioxidant defense system, immune suppression, and metabolic dysfunction. This study provides valuable insights into the molecular responses of S. dumerili to MHWs and supports the selection for thermal resistance in this species.
- Open Access
- 14 March 2025
- Published by MDPI AG in Fermentation
- Vol. 11 (3) , 145
Optimizing Fermentation of Morus nigra L. Residues with Schizophyllum commune to Enhance Anthocyanin Release and Anti-Inflammatory Activity via Pyroptosis Pathway Modulation
Morus nigra L. is rich in anthocyanins and other active ingredients, but its extraction residues pose a burden on the environment. In the present study, Morus nigra L. extraction residue resource utilization was achieved through liquid fermentation of Schizophyllum commune, with the aim of enhancing anthocyanin solubilization and evaluating anti-inflammatory activity. Response surface methodology was used to optimize fermentation parameters and quantify anthocyanin fractions by HPLC. The anti-inflammatory effect was evaluated using the lipopolysaccharide-induced inflammation model of human foreskin fibroblast (BJ cell), and the interaction of cyanidin-3-O-glucoside (C3G) with NLRP3, a key target of the pyroptosis pathway, was resolved by molecular docking. Our results indicated that the optimal conditions (substrate 3.4%, inoculum 9%, time 50 h) enabled the total anthocyanin to reach 85.1 μg/mL, of which the C3G content was elevated to 66.7 μg/mL (release efficiency of 83.9%). The fermented filtrate effectively promoted BJ cell proliferation and inhibited the lipopolysaccharide-induced inflammatory response, with the pyroptosis signaling pathway playing a significant role. Molecular docking confirmed that C3G binds strongly to the NLRP3 protein. This technology provides a new strategy for high-value utilization of Morus nigra L. residues and the development of natural anti-inflammatory drugs.
- 14 March 2025
- Published by MDPI AG in Fermentation
- Vol. 11 (3) , 145
Open AccessOptimizing Fermentation of Morus nigra L. Residues with Schizophyllum commune to Enhance Anthocyanin Release and Anti-Inflammatory Activity via Pyroptosis Pathway Modulation
Morus nigra L. is rich in anthocyanins and other active ingredients, but its extraction residues pose a burden on the environment. In the present study, Morus nigra L. extraction residue resource utilization was achieved through liquid fermentation of Schizophyllum commune, with the aim of enhancing anthocyanin solubilization and evaluating anti-inflammatory activity. Response surface methodology was used to optimize fermentation parameters and quantify anthocyanin fractions by HPLC. The anti-inflammatory effect was evaluated using the lipopolysaccharide-induced inflammation model of human foreskin fibroblast (BJ cell), and the interaction of cyanidin-3-O-glucoside (C3G) with NLRP3, a key target of the pyroptosis pathway, was resolved by molecular docking. Our results indicated that the optimal conditions (substrate 3.4%, inoculum 9%, time 50 h) enabled the total anthocyanin to reach 85.1 μg/mL, of which the C3G content was elevated to 66.7 μg/mL (release efficiency of 83.9%). The fermented filtrate effectively promoted BJ cell proliferation and inhibited the lipopolysaccharide-induced inflammatory response, with the pyroptosis signaling pathway playing a significant role. Molecular docking confirmed that C3G binds strongly to the NLRP3 protein. This technology provides a new strategy for high-value utilization of Morus nigra L. residues and the development of natural anti-inflammatory drugs.
- Open Access
Molecular Mechanism: Inhibition of Fusarium oxysporum T-2 Toxin Synthesis by Surfactin in Dried Fish: Induction of Yap1 Nucleation by ROS Accumulation
(1) T-2 toxin synthesized by Fusarium oxysporum (F. oxysporum) can cause deterioration of dried fish and endanger human health. (2) The molecular mechanism by which antibacterial lipopeptides surfactin inhibited F. oxysporum growth and toxin production was elucidated by investigating the intracellular ROS production pathway and the subcellular distribution and transcriptional activity of the transcription factor Yap1 and its regulation of Tri5 gene in F. oxysporum. (3) Surfactin caused hyphal damage and nucleic acid and protein leakage; thus, the growth of F. oxysporum was disrupted. Surfactin’s excessive accumulation of intracellular ROS triggered the translocation of transcription factor Yap1 into the nucleus, resulting in toxin cluster gene Tri5 expression inhibition, thereby blocking T-2 toxin synthesis. (4) This is a novel mechanism by which surfactin inhibits the growth and T-2 toxin synthesis of F. oxysporum from multiple aspects, including cell structural integrity and the ROS-Yap1 signaling pathway. (5) This study provides a theoretical basis for the application of surfactin in the antifungal control of aquatic dry products.
Open AccessMolecular Mechanism: Inhibition of Fusarium oxysporum T-2 Toxin Synthesis by Surfactin in Dried Fish: Induction of Yap1 Nucleation by ROS Accumulation
(1) T-2 toxin synthesized by Fusarium oxysporum (F. oxysporum) can cause deterioration of dried fish and endanger human health. (2) The molecular mechanism by which antibacterial lipopeptides surfactin inhibited F. oxysporum growth and toxin production was elucidated by investigating the intracellular ROS production pathway and the subcellular distribution and transcriptional activity of the transcription factor Yap1 and its regulation of Tri5 gene in F. oxysporum. (3) Surfactin caused hyphal damage and nucleic acid and protein leakage; thus, the growth of F. oxysporum was disrupted. Surfactin’s excessive accumulation of intracellular ROS triggered the translocation of transcription factor Yap1 into the nucleus, resulting in toxin cluster gene Tri5 expression inhibition, thereby blocking T-2 toxin synthesis. (4) This is a novel mechanism by which surfactin inhibits the growth and T-2 toxin synthesis of F. oxysporum from multiple aspects, including cell structural integrity and the ROS-Yap1 signaling pathway. (5) This study provides a theoretical basis for the application of surfactin in the antifungal control of aquatic dry products.