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Lactic Acid Bacteria: From Bioprocessing to Nanomedicine

  • Maryam Rezvani,
  • Maria Manconi and
  • Nejat Düzgüneş

Background/Objectives: Lactic acid bacteria have long been recognized as pivotal microorganisms in food fermentation and health promotion. However, their significance has recently grown due to innovative applications in various fields, particularly at the intersection of biotechnology and nanotechnology. This study aimed to provide a comprehensive overview of these emerging applications. Methods: The latest scientific literature was drawn from online databases and thoroughly reviewed. The new nomenclature system based on the post-2020 reclassification was used for reports. Results: The current study highlighted the evolving role of lactic acid bacteria, beyond their traditional use as starter cultures for food fermentation, in newer challenges, including the production of high-value bioactive compounds through bioprocessing under optimal conditions to enhance the yield, underlining the involved genes and pathways. Furthermore, this review addressed the beneficial effects of lactic acid bacteria as probiotics, postbiotics, and paraprobiotics in the treatment of various diseases and disorders, their application in the production of functional foods, and the encapsulation of their bioproducts to produce advanced health-promoting functional ingredients. The potential use of lactic acid bacteria to synthesize metallic nanoparticles, minicells, and carbon dots was also explored, promising significant advancements in nanomedicine. Conclusions: This review could open a new horizon for leveraging the potential of lactic acid bacteria in biotechnology, food science, and nanomedicine. The multilateral perspective offered here would provide a foundation for future research and development to exploit the capabilities of lactic acid bacteria across these innovative fields.

27 January 2026

Schematic representation of metabolic pathways of heterofermentative and homofermentative lactic acid bacteria. 1: Hexokinase; 2: Glucose-6-phosphate dehydrogenase; 3: 6-Phosphogluconate dehydrogenase; 4: Ribulose-5-phosphate epimerase; 5: Phosphoketolase; 6: Glyceraldehyde-3-phosphate dehydrogenase; 7: Phosphoglycerate kinase; 8: Phosphoglycerate mutase; 9: Enolase; 10: Pyruvate kinase; 11: Lactate dehydrogenase; 12: Phosphate acetyltransferase; 13: Acetaldehyde dehydrogenase; 14: Alcohol dehydrogenase; 15: Phosphoglucose isomerase; 16: Phosphofructokinase; 17: Aldolase; 18: Triosephosphate isomerase; AcP: Acetyl-phosphate; G3P: Glyceraldehyde-3- phosphate; ACoA: Acetyl-Coenzyme A; DHAP: Dihydroxyacetone-phosphate.

The pharmaceutical industry faces a broken drug development pipeline, characterized by high costs, slow timelines and is prone to high failure rates. The convergence of Artificial Intelligence (AI) and quantum technologies is poised to fundamentally transform this landscape. AI excels in interpreting complex data, optimizing processes and designing drug candidates, while quantum systems enable unprecedented molecular simulation, ultra-sensitive sensing and precise physical control. This convergence establishes an integrated, self-learning ecosystem for the discovery, development, and delivery of therapeutics. This framework co-designs strategies from molecular targeting to formulation stability, compressing timelines and enhancing precision, which may enable safer, faster, and more adaptive medicines.

14 January 2026

Overview of Quantum–Classical Synergy Across the Pharmaceutical R&D and Artificial Intelligence Pipeline. This schematic illustrates how quantum technologies integrate across six stages of drug discovery and development stages (S1–S6). At the center, an Artificial Intelligence (AI) and Quantum Orchestration Layer coordinates with six quantum modules. The Quantum AI layer (blue circle) includes Quantum Simulation, Quantum Analysis, and Quantum Security & Communication, while the Quantum Physical layer (purple circle) comprises Quantum Sensors, Quantum Actuators, and Quantum Security Hardware. Each module includes representative algorithms and devices (e.g., Variational Quantum Eigensolver (VQE)/Density Matrix Embedding Theory (DMET) for simulation, Nitrogen-Vacancy (NV)-center magnetometry for sensing, spin-based actuators for delivery, quantum key distribution (QKD) for secure communication). The pharmaceutical pipeline (as a gray trace with golden-orange diamond markers), spanning Hit Finding, Target/Mechanism, Preclinical, Clinical Development and Post-Market Surveillance. The Provenance Ledger ensures immutable audit trails, while human oversight checkpoints and Agentic AI governance reinforce safety and accountability.

Background: Proper storage of biofluids is critical to preserving their molecular integrity for downstream applications. This study investigates the effect of different storage temperatures on the stability of preservative-free urine samples over a two-year period. Methods: Urine samples were collected, aliquoted, and stored at −80 °C, −20 °C, 4 °C, and in lyophilized form. Samples were retrieved at 0, 6, 12, and 24 months for analysis. DNA, RNA, and protein were isolated and evaluated using agarose and polyacrylamide gel electrophoresis. Nucleic acid quality was assessed using Nanodrop spectrophotometry and Bioanalyzer profiles. Results: A significant increase in pH and a concurrent decline in protein concentration were observed within the first six months at −20 °C and 4 °C. These changes plateaued after six months. Samples stored at −80 °C and in lyophilized form showed minimal variation in pH and retained higher protein stability. DNA quality, based on 260/280 and 260/230 ratios and electrophoretic band integrity, was well-preserved under these two conditions. RNA quality remained stable for up to 12 months but declined thereafter. Conclusions: Storage at −80 °C or in lyophilized form offers optimal preservation of protein concentration and nucleic acid quality in preservative-free urine samples over extended storage durations. However, lyophilization offers a cost-effective and logistically practical alternative, as samples can be stored at room temperature without the requirement of ultra-low freezers.

25 December 2025

Workflow of Study—30–50 mL urine samples were collected, and 2–10 mL aliquots were prepared and stored at four different temperatures (−80 °C, −20 °C, 4 °C, and RT in lyophilized form). Evaluation of all parameters was conducted at four time points: at the time of collection (T0), after 6 months of storage (T6), after 12 months of storage (T12), and after 24 months of storage (T24) at all storage temperatures.

Background/Objectives: Acute myeloid leukemia (AML) is the most common acute leukemia in adults, with over 50% of individuals succumbing to the disease annually. This study aimed to assess the correlation between human leukocyte antigen (HLA) genes and acute myeloid leukemia (AML) in an adult Moroccan cohort. We included 60 persons with acute myeloid leukemia (AML) who were eligible for hematopoietic stem cell transplantation and compared them to a control group of 90 healthy adults. Methods: Patients and controls were subjected to HLA class I and II typing utilizing either sequence-specific primers (SSP) or sequence-specific oligonucleotides (SSO) in polymerase chain reaction-based methodologies. Results: The AML categories were predominantly represented by AML2, AML3, and AML4, comprising 36.66%, 30%, and 16.66%, respectively. We identified a notable correlation between HLA-A*11 (p = 0.003) and HLA-B*27 (p = 0.005) with acute myeloid leukemia (AML), and for HLA class II allele groups, we detected an elevated frequency of HLA-DQB1*05 (p = 0.002) in adult AML patients. We identified a notable correlation between AML 2 and the allele groups examined, namely with HLA class I: HLA-A*11 (p = 0.0003) and HLA-B*27 (p = 0.00006). Conclusion: Our study suggests a potential association between specific HLA alleles and the development of AML specifically AML type 2 in adults. Further larger studies are needed to confirm these findings.

3 December 2025

Comparative frequency of HLA-A*11, B*27, and DQB1*05 between adult patients with AML and controls.

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BioChem - ISSN 2673-6411