Hamed Hamouda is employed at the Processes Design & Development Department of the Egyptian Petroleum Research Institute (EPRI) in Cairo, Egypt. He obtained his master's degree in Microbiology from Al-Azhar University's faculty in May 2015, followed by a Ph.D. in Microbiology from the University of Chinese Academy of Sciences in 2020. From January 2021 to June 2023, he worked as a postdoctoral researcher at the food security and molecular microbiology group at the College of Food Science and Engineering, Ocean University of China, Qingdao, China. Currently, Hamouda is engaged in postdoctoral research at the Natural Products and Sugar Engineering Research Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences.
I have been interested in biochemical research related to protein and carbohydrate interactions throughout my academic career. My Ph.D. research focused on the expression and characterization of novel polysaccharide degrading enzymes, particularly pectate lyases,
RESEARCH, TEACHING, or OTHER INTERESTS
Renewable Energy, Sustainability and the Environment, Food Science, Biochemistry, Genetics and Molecular Biology, Structural Biology
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Scopus Publications
Scopus Publications
Recent molecular insights and biosensor-based diagnostic technologies for hyperphosphorylated Tau in Alzheimer's disease Samah Shabana, Hamed I. Hamouda, Angyang Shang, Shuai Shao, Jinyuan Zhao, Hong Yuan, Bo Liu Alzheimer S Research and Therapy, 2026 Tau pathology is a defining feature of Alzheimer's disease (AD), with hyperphosphorylated Tau (p‑Tau) emerging as a central biomarker for early diagnosis and disease monitoring. Various p‑Tau epitopes have demonstrated superior diagnostic precision and now form the molecular basis of updated AD diagnostic frameworks. Classical immunoassays such as enzyme-linked immunosorbent assay (ELISA), chemiluminescent enzyme immunoassay (CLEIA), and single molecule array (SIMOA) remain central to fluid based detection, offering high sensitivity and clinical validation. Recent advances in tau biology, especially in post-translational modifications, have driven the development of next generation biosensors. Electrochemical, optical, and nanostructured platforms now enable real-time, label-free, and attomolar level detection of p‑Tau in biofluids and live cell models. These systems are increasingly portable and suitable for point of care or in vivo applications. This review highlights the evolution of p‑Tau detection technologies, from benchmark immunoassays to cutting edge biosensors. Special attention is given to advanced affinity reagents, including aptamers, synthetic peptides, and antibody mimetics, which enhance biosensor specificity, stability, and translational potential. Together, these innovations are redefining AD diagnostics, enabling early intervention and more effective disease monitoring.
Enhancing the Catalytic Properties of a Novel Bifunctional κ-Carrageenanase through Spontaneous Self-Cyclization Based on the SpyTag/SpyCatcher System Zhe Wang, Suxue Chen, Yan Li, Yu Xin, Chunhui Liu, Haipeng Su, Hamed I. Hamouda, Mohamed A. Balah, Yongjun Mao, Hong Jiang, Xiangzhao Mao Journal of Agricultural and Food Chemistry, 2026 Furcellaran is a distinct carrageenan polysaccharide. The unique oligosaccharides produced by its degradation exhibit lower sulfate group content and play a crucial role in elucidating the structure–activity relationship of carrageenan oligosaccharides. In this study, a novel κ-carrageenanase OUC-CgkA-Sn from Stieleria neptunia was identified to display dual substrate hydrolysis activity against κ-carrageenan and furcellaran. Significantly, the furcellaran-degrading activity of OUC-CgkA-Sn was 1.77-fold higher than that toward κ-carrageenan, and the primary degradation product was desulfurized κ-neocarrahexaose. To enhance its catalytic properties, the SpyTag/SpyCatcher system was employed to construct the fusion enzyme CKT, which is capable of spontaneous self-cyclization in vitro . After cyclization, CKT exhibited a dual enhancement in stability and enzyme activity simultaneously: 193.61% higher half-life and 195.21% greater enzyme activity. Spatial structure analysis revealed that this enhancement stemmed from increased structural stability and strengthened substrate interactions. As a result, CKT holds great promise for the efficient preparation of structurally diverse carrageenan oligosaccharides.
Characterization and Functional Mechanism Analysis of Two Glycoside Hydrolase Family-39 β-Xylosidases Identified from Caldicellulosiruptor saccharolyticus Hang Su, Wenjie Han, Hamed I. Hamouda, Huidan Zhang, Ming Lu Journal of Agricultural and Food Chemistry, 2026 β-Xylosidase, crucial for xylan degradation, catalyzes xylose release from xylo-oligosaccharides. However, enzymatic characters of β-xylosidases possess certain limitations, including poor thermal stability, and inhibitors are unclear. This study identified two GH39 family β-xylosidases, Cs Xyl39A and Cs Xyl39B, from the thermophilic bacterium Caldicellulosiruptor saccharolyticus . Both enzymes exhibited exceptional thermostability and compatibility with organic solvents, making them promising for industrial applications. Cs Xyl39A specifically cleaved d -xylopyranosyl groups from substrates such as notoginsenoside R1 and p -nitrophenyl-β- d -xylopyranoside. The catalytic efficiency in organic-solvent/water-miscible (O/Wm) systems was enhanced, and the physical immobilization on macroporous polystyrene strengthened its resistance to organic solvents in high-ratio O/Wm solutions. Cs Xyl39B demonstrated high specific activity and thermal stability at 70 °C, maintaining a 26 h half-life while producing xylose and glucose, indicating its suitability for lignocellulose biodegradation. Together, these enzymes address key industrial challenges, offering enhanced stability and solvent adaptability for sustainable bioprocessing applications.
High Value Utilization of Sugar and Starch Industry Waste by Biotechnological Approaches Biotechnological Approaches for Sustainable Environment Management, 2025
Exploiting marine phospholipid nanoliposomes for enhanced apremilast delivery and therapeutic efficacy in inflammatory bowel disease Samah Shabana, Hamed I. Hamouda, Heng Yin, Samia Hamouda, Busati Ahmed, Mohamed H. El-Sayed, Zhe Chi, Chenguang Liu Colloids and Surfaces A Physicochemical and Engineering Aspects, 2025 Marine phospholipid (MPL) nanoliposomes represent a new frontier in drug delivery systems , offering unique bio-functional and physicochemical properties. This study developed orally administered MPL nanoliposomes to enhance apremilast delivery and bioavailability in inflamed bowel disease (IBD). Drug release studies showed effective gastric protection (21.2 ± 0.4 % release at pH 1.2 after 2 h) and substantial release (96.4 ± 0.3 %) at pH 6.8 over 12 h. The optimized formulation (4 % drug w/w) showed remarkable stability over 6 weeks of storage at 4 °C. Apr/MPL nanoliposomes up to 300 µg/mL showed great cytocompatibility to RAW 264.7 macrophages and Caco2 intestinal cells. Furthermore, the formulation exhibited superior anti-inflammatory effects, significantly reducing nitric oxide (NO) production and downregulating pro-inflammatory cytokines (TNF-α, IL-1β, IL-6) in lipopolysaccharide (LPS)-stimulated RAW 264.7 macrophages. In vivo , Apr/MPL nanoliposomes improved recovery in a dextran sulfate sodium (DSS)-induced ulcerative colitis model, outperforming free apremilast . These findings underscore MPL nanoliposomes as a promising pharmacological tool for managing inflammation and a versatile drug delivery system for IBD.
Marine phospholipid nanoliposomes mediate oral colonic delivery of 5-aminosalicylic acid and mitigate the severity of DSS-induced colitis in mouse models Samah Shabana, Hamed I. Hamouda, Suzan Noureldin, Zhe Chi, Chenguang Liu Journal of Drug Delivery Science and Technology, 2025 5-Aminosalicylic acid (5-ASA) is the preferred medication for treating mild to moderate inflammatory bowel disease (IBD). However, side effects and sometimes insufficient efficacy pose challenges. This study introduces chitosan-coated orally targeted marine phospholipid nanoliposomes grafted with Vit. E. TPGS for delivering 5-aminosalicylic acid to the inflamed mucosa in IBD treatment. MTL nanoliposomes were prepared by the thin film hydration method, exhibiting sizes of 165.8 ± 2.19 nm pre-coating and 259.5 ± 1.77 nm size post-coating. The nanoliposomes showed controlled drug release at intestinal pH, with minimal release in the simulated gastric medium. They demonstrated excellent stability over a 45-day storage period. In vitro , cytocompatibility studies with L929 cells and ex vivo studies with RBCs showed excellent biocompatibility . MTL nanoliposomes showed selective deposition in inflamed RAW 264.7 macrophages and time-dependent uptake in Caco2 intestinal cells. In vitro, anti-inflammatory experiments significantly reduced inflammatory biomarkers like TNF-α, IL1-β, IL-6, and ROS. In vivo, DSS-induced colitis studies demonstrated improved colitis indices, colonic tissue change restoration, and myeloperoxidase activity inhibition. These findings underscore the potential of MTL nanoliposomes as a promising targeted delivery system for 5-aminosalicylic acid in treating IBD. • Marine phospholipid nanoliposomes were effective in hydrophilic drug encapsulation. • MPL nanoliposomes demonstrated a synergistic effect, enhancing drug efficacy and therapeutic outcomes. • Marine phospholipid nanoliposomes offer breakthrough potential for drug delivery in inflammatory bowel disease (IBD).
Mining of Novel Myrosinase with High Activity Based on Sequence and Structure Clustering for Efficient Preparation of Sulforaphane Jiaqi Wang, Hong Jiang, Suxue Chen, Yan Li, Zhe Wang, Hamed I. Hamouda, Mohamed A. Balah, Changhu Xue, Xiangzhao Mao Journal of Agricultural and Food Chemistry, 2025 Sulforaphane has garnered significant research attention owing to its potent and promising biological activities. Mining the highly active myrosinase is the key to preparing sulforaphane. In this study, a novel myrosinase, designated Semyr, was identified from Serratia plymuthica through sequence and structural clustering analysis. The enzyme was heterologously expressed in Escherichia coli, demonstrating a sinigrin hydrolysis activity of 110.48 U/mg, which constitutes the highest recombinant myrosinase activity reported to date. A reaction system was established to prepare sulforaphane. 60 U of myrosinase was added to 5 mL of substrate, yielding 15.39 mg of sulforaphane per gram of broccoli seeds after 20 min at 40 °C and pH 6.0, with a conversion rate of 96.50%. Concurrently, the highest productivity of 5.55 μmol/g·min for sulforaphane was achieved after 15 min. Thus, Semyr serves as a valuable biocatalytic tool for the efficient preparation of sulforaphane.
Statistical optimization of batch ethanol fermentation of sugarcane molasses by Candidatropicalis strainHSC-24 International Journal of Chemtech Research, 2015
