Search Results (860)

MicroRNAs (miRNAs) are key post-transcriptional regulators of plant development and stress responses, with many being conserved across diverse plant lineages. In this study, we investigated the expression profiles of miRNAs and their corresponding target genes in Arachis stenosperma, a wild peanut relative that exhibits robust resistance to root-knot nematodes (RKN). Small RNA sequencing of nematode-infected roots identified 107 miRNA loci, of which 93 corresponded to conserved miRNA families and 14 represented novel candidates, designated as miRNOVO. Among these, 18 miRNAs belonging to 11 conserved families were identified as differentially expressed (DEMs). Notably, miR399 and miR319 showed the highest upregulation (logFC = 4.25 and 4.20), while miR393 and miR477 were the most downregulated (logFC = −0.83 and −0.79). Integrated analysis of miRNA and transcriptome data revealed several regulatory interactions involving key defense-related genes. These included NLR genes targeted by miR393 and miR477, hormone signaling components such as the auxin response factor ARF8 targeted by miR167, and the growth regulator GRF2 targeted by miR396. Additionally, miR408 was predicted to target laccase3, a gene involved in the oxidation of phenolic compounds, lignin biosynthesis, copper homeostasis and defense responses. Remarkably, four immune receptor genes belonging to the nucleotide-binding site leucine-rich repeat (NLR) family displayed inverse expression patterns relative to their regulatory miRNAs, suggesting miRNA-mediated post-transcriptional control during the early stages of nematode infection. These findings reveal both conserved and species-specific miRNA–mRNA modules associated with nematode resistance in A. stenosperma, highlighting promising targets for developing RKN-tolerant peanut cultivars through miRNA-based strategies. Full article

Drought stress severely limits peanut productivity, highlighting the urgent need to understand the molecular mechanisms that underlie drought adaptation. While microRNAs (miRNAs) are known to play essential roles in plant stress responses, their functional contributions in polyploid crops like peanut remain insufficiently explored. This study provides the first integrated transcriptomic analysis of drought-responsive miRNAs in tetraploid peanut (Arachis hypogaea). We performed high-throughput sRNA sequencing on a drought-tolerant cultivar Fenhua 8 under PEG6000-simulated drought stress, identifying 10 conserved drought-responsive miRNAs. Among these, ahy-miR398 and ahy-miR408 were significantly downregulated under drought conditions. Degradome sequencing revealed that ahy-miR398 targets copper chaperones for superoxide dismutase (CCSs), potentially reducing SOD activation and amplifying oxidative stress. In contrast, ahy-miR408 targets laccase 12 (LAC12), P-type ATPase copper transporters (COPAs), and a blue copper protein-like (PCL) gene. These targets are involved in copper homeostasis and the regulation of reactive oxygen species (ROS), suggesting that ahy-miR408 plays a role in oxidative stress management. Functional validation in transgenic Arabidopsis lines overexpressing ahy-miR398 or ahy-miR408 showed significantly reduced drought tolerance, with impaired seed germination, shorter primary roots, and exacerbated growth suppression during water deprivation. Taken together, these findings highlight a novel miRNA-mediated regulatory network in peanut drought adaptation, centered on copper-associated oxidative stress management. This study provides new insights into miRNA-based regulation in polyploid crops and offers potential molecular targets for breeding climate-resilient peanut varieties, especially in arid regions where yield stability is crucial. Full article

Mushroom diversity is essential for maintaining ecological balance and provides valuable bioactive compounds for human use. Beyond their nutritional value, mushrooms contribute to functional foods and have applications in nutraceuticals, pharmaceuticals, and biotechnology. For example, β-glucans from Lentinula edodes are commercialized as immune-enhancing nutraceuticals, polysaccharide Krestin (PSK) from Trametes versicolor is used as an adjuvant in cancer therapy, and enzymes such as laccases from Pleurotus species are widely applied in biotechnological processes. One of the abundant compounds found in mushrooms is ergosterol, which is a sterol present in the cell membrane of the fungal body. Ergosterol has significant health benefits due to its antioxidant, immunomodulatory, and anti-inflammatory properties. Furthermore, ergosterol is a precursor to vitamin D₂ (ergocalciferol), which can be synthesized through exposure to ultraviolet (UV) light and thermal radiation. This review highlights the importance of Himalayan mushroom biodiversity, particularly the wild edible mushrooms traditionally collected and used. This review thoroughly discusses the ergosterol and vitamin D₂ content, their biosynthesis in mushrooms, and the role of environmental factors used to enhance biosynthesis. We also discuss the sustainable cultivation of Himalayan mushrooms and their nutraceutical properties. Several Himalayan mushrooms have been reported to possess health-promoting properties, and their incorporation into functional foods may contribute to improved public health. Furthermore, the future research directions are highlighted. Full article

Fungal laccases oxidize a wide range of substrates with a diverse spectrum of subsequent non-specific free radical reactions, leading to the production of unwanted byproducts. This work describes a unique recombinant alkaliphilic laccase from Paramyrothecium roridum VKM F-3565 capable of performing specific oligomerization of phenylpropanoids (precursors of natural lignin and lignans) in a neutral environment, thus preventing the reverse reaction of depolymerization which occurs in an acidic environment. The recombinant alkaliphilic laccase from P. roridum VKM F-3565 with a specific enzyme activity of about 154.0 U/mg (in the reaction with 1 mM ABTS) was obtained using a Komagataella phaffii transformant with a yield of 20 ± 1.5 mg/L. The recombinant laccase had an increased degree of N-glycosylation (MW = 97 kDa), higher pH optimum in reaction with phenylpropanoids and a decreased temperature optimum, compared to the wild-type laccase. The enzyme exhibited great resistance to surfactants and the EDTA in the neutral conditions rather than the acidic ones, whereas its tolerance to mono- and divalent-metal ions was high at acidic conditions. This work demonstrates the important role of N-glycosylation of the alkaliphilic laccase of P. roridum VKM F-3565 in its functional activity. The presence of pH-dependent reactions makes the studied laccase attractive for the phenylpropanoid oligomerization with the production of novel oligomeric phenylpropanoid derivatives for industrial and pharmacological purposes. Full article

Pleurotus ostreatus is one of the most frequently cultivated mushroom species. It has attracted considerable attention not only because of its short cultivation time, but also because of the wide range of substrates on which it can be cultivated, such as lignocellulosic materials, synthetic polymers and wastewater. The popularity of the oyster mushroom stems not only from its rapid growth and high adaptability, but also from its functional ingredients, which include laccase, proteoglycan and β-glucan. As understanding the molecular biology of Pleurotus ostreatus is crucial for evaluating its commercial and scientific applications, modern molecular tools have been used to search for the genes and proteins involved in the development of this mushroom and production of valuable metabolites. The rapid development of artificial intelligence may make it possible to automate and optimize the entire cultivation process of Pleurotus ostreatus. This report summarizes the cultivation of Pleurotus ostreatus using waste raw materials, the nutritional and medicinal value for applications, transcriptomic and proteomic analyses and the use of artificial intelligence systems. In addition, future perspectives are discussed to make the cultivation of Pleurotus ostreatus environmentally friendly and to ensure an increase in its productivity and quality. Full article

Tetracycline antibiotics are widely used, but their resistance to degradation and persistence in the environment pose a potential risk of inducing antibiotic resistance, creating significant threats to both the environment and human health. This study established a laccase–mediator system (LMS) using natural green tea polyphenols (GTPs) as mediators for efficient tetracycline degradation. Through analyzing the main GTP components and optimizing the reaction conditions, the degradation efficiency of the system was evaluated. The experimental results indicated that, among the various tea polyphenol components, epicatechin gallate (ECG) contributed the most significantly to the degradation efficiency. Under optimized conditions, the Lac-ECG system degraded over 98% of tetracycline within 3–4 min. Further optimization of the Lac-GTP system allowed us to identify the following optimal conditions: a GTP concentration of 1.0 mmol/L, laccase concentration of 1.0 mg/mL, pH of 6.0, and temperature of 25 °C. Under these conditions, a degradation rate of 95.07% was attained within 5 min, outperforming a system using the synthetic mediator ABTS. Additionally, metal ions such as Ca²⁺, Mg²⁺, Cu²⁺, Fe³⁺, Fe²⁺, and Ni²⁺ were found to enhance the degradation process, while Mn²⁺ and Hg²⁺ exhibited inhibitory effects. Antibacterial activity tests revealed that the degradation products completely lost their antimicrobial activity, demonstrating effective detoxification of tetracycline. In conclusion, the tea polyphenol-based laccase–mediator system developed in this study exhibits high efficiency, cost-effectiveness, and environmental friendliness, offering a promising strategy for the remediation of tetracycline-contaminated environments. Full article

Fungal laccases are promising oxidative enzymes for bioremediation applications, particularly in the degradation of synthetic dyes present in industrial effluents. Here, we evaluated the inhibitory effects of sodium chloride (NaCl) and sodium sulfate (Na₂SO₄) on the activity of Trametes versicolor laccase and its ability to decolorize Congo Red (CR), Malachite Green (MG), and Remazol Brilliant Blue R (RBBR). Enzyme assays revealed concentration-dependent inhibition, with IC₅₀ values of 0.22 ± 0.04 M for NaCl and 1.00 ± 0.09 M for Na₂SO₄, indicating stronger inhibition by chloride. Kinetic modeling showed mixed-type inhibition for both salts. Despite this effect, the enzyme maintained significant activity: after 12 h, decolorization efficiencies reached 95 ± 4.0% for MG, 88 ± 3.0% for RBBR, and 75 ± 3.0% for CR, even in the presence of 0.5 M salts. When applied to a mixture of the three dyes, decolorization decreased only slightly in saline medium (94.04 ± 4.0% to 83.43 ± 5.1%). FTIR spectra revealed minor structural changes, but toxicity assays confirmed marked detoxification, with radicle length in lettuce seeds increasing from 20–38 mm (untreated dyes) to 41–48 mm after enzymatic treatment. Fungal growth assays corroborated reduced toxicity of treated dyes. These findings demonstrate that T. versicolor laccase retains functional robustness under ionic stress, supporting its potential application in saline textile wastewater remediation. Full article

Breast cancer remains a leading cause of morbidity and mortality among women globally, with increasing incidence projected in the coming years. Despite advances in standard oncologic therapies, there is a growing interest in supportive interventions that enhance treatment efficacy and reduce adverse effects. This review critically evaluates preclinical and clinical data on the medicinal mushroom Coriolus versicolor and its bioactive compounds—primarily polysaccharide-K, polysaccharopeptide, and laccase—as potential adjuvants in breast cancer therapy. A systematic PubMed search identified 11 original studies from 2010 to 2025 examining the impact of C. versicolor on breast cancer cell lines, animal models, and human subjects. Findings consistently demonstrate antiproliferative, pro-apoptotic, necroptotic, anti-invasive, and immunomodulatory effects across various breast cancer subtypes, including triple-negative breast cancer. One phase I clinical trial also reported good tolerability and immunological benefits in patients post-chemotherapy. The review highlights molecular mechanisms involving apoptosis, necroptosis, and modulation of the tumor microenvironment. While promising, these results underscore the need for standardized preparations, pharmacokinetic data, and larger placebo-controlled trials. Overall, C. versicolor shows potential as a safe, natural adjunct to conventional therapy, offering prospects for integrative strategies in breast cancer management. Full article

Natural laccase is an environmentally friendly biocatalyst in the degradation of a broad range of toxic pollutants because its catalysis reaction does not require or produce toxic reactants and byproducts. However, its inherent limitations, such as operational sensitivity, poor stability, and difficulty in recovery/reusability, have significantly restricted its practical environmental applications. Consequently, in recent years, researchers have focused on the development of sustainable catalysts to mimic natural laccase. This review focuses on biomolecule-based laccase mimics, which are derived from nucleotides, nucleic acids, amino acids, peptides, and proteins, summarizing their environmental applications. These biomolecule-based laccase mimics not only overcome the limitations of natural laccase by offering advantages such as high stability, ease of recycling, and long-term storage but also exhibit excellent biodegradability, making them green and sustainable catalytic materials. This study aims to present recent progress in biomolecule-based laccase mimics, as well as their challenges, and to offer future directions in laccase-like catalysts for environmental applications. Full article

The relationship between the structure and function of bacterial laccases has garnered significant research attention thanks to their straightforward molecular structure. Nevertheless, studies examining the impact of an altered molecular structure on the heterologous expression of bacterial laccases in Escherichia coli remain scarce. Our research focuses on elucidating the impact of incorporating copper ions into the molecular structure of modified CotA on its exogenous expression in E. coli as well as its impact on the significance of the amino acid residues surrounding the internal electron channels and water molecule channels of the enzyme molecule. The results show that single-site mutation may affect the expression of CotA by affecting its soluble expression with different binding capacities for copper ions. In addition, the mutants exhibited different laccase activity levels. The catalytic efficiency of T466A was found to be significantly enhanced, reaching 2.29 times that of the wild type. We used structural models to illustrate the correlation between molecular structure and function after the replacement of three mutation sites with alanine. The reduction of hydrogen bonds may be an important factor influencing Cu²⁺’s binding ability and the water molecule production rate. The T466A mutant exhibited strong decolorization ability for Reactive Blue 19 and Eriochrome Black T with 42.2% and 58.2% decolorization rates after one hour of reaction, respectively. This study demonstrates that the molecular mutation studied influences the CotA expression level, enzyme activity, and dye decolorization. Full article

Laccases, a class of multicopper oxidases found in diverse biological sources, have emerged as key green biocatalysts with significant potential for eco-friendly pollutant degradation. Their ability to drive electron transfer reactions using oxygen, converting pollutants into less harmful products, positions laccases as promising tools for scalable and sustainable treatment of wastewater, soil, and air pollution. This review explores laccase from a translational perspective, tracing its journey from laboratory discovery to real-world applications. Emphasis is placed on recent advances in production optimization, immobilization strategies, and nanotechnology-enabled enhancements that have improved enzyme stability, reusability, and catalytic efficiency under complex field conditions. Applications are critically discussed for both traditional pollutants such as synthetic dyes, phenolics, and pesticides and emerging contaminants, including endocrine-disrupting chemicals, pharmaceuticals, personal care products, microplastic additives, and PFAS. Special attention is given to hybrid systems integrating laccase with advanced oxidation processes, bioelectrochemical systems, and renewable energy-driven reactors to achieve near-complete pollutant mineralization. Challenges such as cost–benefit limitations, limited substrate range without mediators, and regulatory hurdles are evaluated alongside solutions including protein engineering, mediator-free laccase variants, and continuous-flow bioreactors. By consolidating recent mechanistic insights, this study underscores the translational pathways of laccase, highlighting its potential as a cornerstone of next-generation, scalable, and eco-friendly remediation technologies aligned with circular bioeconomy and low-carbon initiatives. Full article

Micro- and nanoplastics (MPs and NPs) are recognized as emerging contaminants posing potential risks to human health. Recent evidence highlights the potential of food-grade microbial strains to bind these particles and facilitate their removal, suggesting a promising probiotic-based strategy for mitigating their adverse health effects. This study investigated the adsorption and biodegradation capabilities of Bacillus subtilis DCP04, a strain isolated from Korean fermented soybean paste, cheonggukjang, on low-density polyethylene (LDPE) particles. Biofilm formation assays and morphological observations confirmed the strain’s ability to adhere to the surface of LDPE. Subsequent experiments demonstrated that DCP04 effectively adsorbed LDPE particles in a size-, time-, and concentration-dependent manner. This interaction induced significant morphological changes and increased hydrophilicity on the polymer surface. Furthermore, a positive correlation was observed between the activities of laccase and manganese peroxidase and a measurable weight loss in LDPE films, suggesting direct enzymatic involvement in polymer degradation. Crucially, the DCP04 strain also met key safety and functional criteria for use as a probiotic. These findings highlight the potential of DCP04 strain as a functional probiotic agent for mitigating the accumulation of MPs and NPs within the human body. Full article

Lignin, the most abundant aromatic biopolymer, represents a key renewable feedstock for sustainable biorefineries, yet its structural complexity poses a formidable challenge for enzymatic degradation. While ligninolytic enzymes such as laccases (LACs), lignin peroxidases (LiPs), and manganese peroxidases (MnPs) exhibit remarkable catalytic versatility, the molecular mechanisms underlying their ability to balance substrate specificity and structural flexibility remain unresolved. Here, we employed all-atom molecular dynamics (MD) simulations and virtual mutagenesis to dissect the dynamic interactions between these enzymes and lignin model compound (β-O-4-linked H-type dimers). Our simulations revealed a dual recognition mechanism in which polar residues (such as Asp, Glu, Arg and His) formed hydrogen bonds with hydroxyl and keto groups near catalytic cleavage sites, ensuring precise alignment for bond scission, while aromatic residues stabilized diverse lignin conformations via hydrophobic interactions with conserved aromatic rings. Conformational dynamics of active-site residues enabled adaptive adjustments to substrate heterogeneity, reconciling enzymatic specificity with structural promiscuity. Virtual mutation experiments further demonstrated that aromatic residues were indispensable for binding stability, whereas polar residues dictated cleavage-site selectivity. These findings provide atomic-scale insights into the catalytic mechanism of ligninolytic enzymes, with implications in the rational design of superior biocatalyst for lignin biorefineries. Full article

Natural deep eutectic solvents (NADES) are produced by combining natural compounds, such as sugars, amino acids, or organic acids, to form a liquid at room temperature. Compared to other solvents, NADES own several strengths, including cost-effectiveness, ease of preparation, tunable properties, biorenewability, and biodegradability, making them suitable for a wide range of industrial sectors. Research on NADES requires careful consideration of their composition and physicochemical properties, as these can significantly influence their range of applications. In this context, the main objective of this review is to provide insights into the application of NADES in different areas that go from enzymatic processes and extraction of bioactives to the formulation of pharmaceutical and cosmetic products. This review includes several case studies on the use of enzyme–NADES systems (lipase and laccase) to synthesize new materials and on the extraction of bioactives with NADES, highlighting their direct application in cosmetics and pharmaceutical formulations. Full article

The efficient degradation of lignin from agricultural by-products is a critical step in the development of sustainable bioprocessing technologies for waste valorisation. Enzymatic degradation of kraft lignin performed with lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase (Lac) was investigated. A response surface methodology (RSM) based on a Box–Behnken Design (BBD) was employed in order to optimise key process parameters including enzyme concentration, lignin concentration, pH, incubation temperature, and activator concentration. The surface plots were used to determine the best conditions for each enzyme in order to better degrade kraft lignin. Therefore, LiP needed a stronger acidic environment and moderate temperature, MnP needed an almost neutral pH and moderate temperature, and Lac needed a neutral pH and higher temperature. This work contributes to the development of smart agricultural waste management practices by combining enzymatic treatments with statistical modelling for process optimisation. This study provides a framework for lignin degradation that can be used as a starting point for diverse lignocellulosic by-product fragmentation, thus supporting a circular bioeconomy initiative in accordance with today’s trends. The optimised enzymatic parameters could help enhance efficiency, enable process standardisation across feedstocks, and support economically and environmentally sustainable industrial-scale lignin valorisation in integrated biorefineries. Full article