Search Results (600)

The sugarcane industry plays a crucial economic role worldwide, with sucrose and ethanol as its main products. However, its processing generates large volumes of by-products—such as bagasse, molasses, vinasse, and straw—that contain valuable components for biotechnological valorization. This review integrates approximately 100 original research articles published in JCR-indexed journals between 2015 and 2025, of which over 50% focus specifically on sugarcane-derived agroindustrial residues. The biotechnological approaches discussed include submerged fermentation, solid-state fermentation, enzymatic biocatalysis, and anaerobic digestion, highlighting their potential for the production of biofuels, enzymes, and high-value bioproducts. In addition to identifying current advances, this review addresses key technical challenges such as (i) the need for efficient pretreatment to release fermentable sugars from lignocellulosic biomass; (ii) the compositional variability of by-products like vinasse and molasses; (iii) the generation of metabolic inhibitors—such as furfural and hydroxymethylfurfural—during thermochemical processes; and (iv) the high costs related to inputs like hydrolytic enzymes. Special attention is given to detoxification strategies for inhibitory compounds and to the integration of multifunctional processes to improve overall system efficiency. The final section outlines emerging trends (2024–2025) such as the use of CRISPR-engineered microbial consortia, advanced pretreatments, and immobilization systems to enhance the productivity and sustainability of bioprocesses. In conclusion, the valorization of sugarcane by-products through biotechnology not only contributes to waste reduction but also supports circular economy principles and the development of sustainable production models. Full article

Fungal lytic polysaccharide monooxygenases (LPMOs) have revolutionized the field of biomass degradation by introducing an oxidative mechanism that complements traditional hydrolytic enzymes. These copper-dependent enzymes catalyze the cleavage of glycosidic bonds in recalcitrant polysaccharides such as cellulose, hemicellulose, and chitin, through the activation of molecular oxygen (O₂) or hydrogen peroxide (H₂O₂). Their catalytic versatility is intricately modulated by structural features, including the histidine brace active site, surface-binding loops, and, in some cases, appended carbohydrate-binding modules (CBMs). The oxidation pattern, whether at the C1, C4, or both positions, is dictated by subtle variations in loop architecture, amino acid microenvironments, and substrate interactions. LPMOs are embedded in a highly synergistic fungal enzymatic system, working alongside cellulases, hemicellulases, lignin-modifying enzymes, and oxidoreductases to enable efficient lignocellulose decomposition. Industrial applications of fungal LPMOs are rapidly expanding, with key roles in second-generation biofuels, biorefineries, textile processing, food and feed industries, and the development of sustainable biomaterials. Recent advances in genome mining, protein engineering, and heterologous expression are accelerating the discovery of novel LPMOs with improved functionalities. Understanding the balance between O₂- and H₂O₂-driven mechanisms remains critical for optimizing their catalytic efficiency while mitigating oxidative inactivation. As the demand for sustainable biotechnological solutions grows, this narrative review highlights how fungal LPMOs function as indispensable biocatalysts for the future of the Circular Bioeconomy and green industrial processes. Full article

The majority of studies of fungal utilization of chitosan are associated with the production of a specific enzyme, chitosanase, which catalyzes the hydrolytic cleavage of the macrochain. In our opinion, the development of approaches to obtaining materials with new functional properties based on non-destructive chitosan transformation by living organisms and their enzyme systems is promising. This study was conducted using a wide range of classical and modern methods of microbiology, biochemistry, and physical chemistry. The ability of the ascomycete Fusarium oxysporum Schltdl. to modify films of chitosan with average-viscosity molecular weights of 200, 450, and 530 kDa was discovered. F. oxysporum was shown to use chitosan as the sole source of carbon/energy and actively overgrew films without deformations and signs of integrity loss. Scanning electron microscopy (SEM) recorded an increase in the porosity of film substrates. An analysis of the FTIR spectra revealed the occurrence of oxidation processes and crosslinking of macrochains without breaking β-(1,4)-glycosidic bonds. After F. oxysporum growth, the resistance of the films to mechanical dispersion and the degree of ordering of the polymer structure increased, while their solubility in the acetate buffer with pH 4.4 and sorption capacity for Fe²⁺ and Cu²⁺ decreased. Elemental analysis revealed a decrease in the nitrogen content in chitosan, which may indicate its inclusion into the fungal metabolism. The film transformation was accompanied by the production of extracellular hydrolase (different from chitosanase) and peroxidase, as well as biosurfactants. The results obtained indicate a specific mechanism of aminopolysaccharide transformation by F. oxysporum. Although the biochemical mechanisms of action remain to be analyzed in detail, the results obtained create new ways of using fungi and show the potential for the use of Fusarium and/or its extracellular enzymes for the formation of chitosan-containing materials with the required range of functional properties and qualities for biotechnological applications. Full article

Fungal communities in high plateau ecosystems remain understudied despite their crucial roles in soil ecosystems, and yeasts inhabiting extreme regions have potential for industrial and biotechnological applications. We studied the fungal diversity in soils across 14 Chilean Altiplano sites using amplicon-based metagenomics and isolation of yeasts to assess their growth under various conditions and hydrolytic enzyme secretion. Using the metagenomic approach, the Ascomycota and Basidiomycota phyla were found to be the most abundant (85% and 8%, respectively). Unclassified families and genera prevailed at six and ten sites, respectively. At the other sites, the most abundant families included Cladosporiaceae, Teratosphaeriaceae, and Sporormiaceae, and the genera Oleoguttula, Coniochaeta, and Peziza. Biodiversity indices did not correlate with the soil’s geographic origin, organic matter content, humidity, or pH. Most isolated yeasts belong to the Naganishia, Holtermanniella, and Vishniacozyma genera, growing at temperatures ranging from 4 °C to 26 °C. Most isolates could use glucose, sucrose, and maltose as carbon sources and exhibited amylase, esterase, pectinase, and protease activities at 30 °C and below. Our results indicate that the evaluated soil physicochemical parameters do not explain the fungal distribution in the Altiplano and highlight the region as a reservoir of unknown fungi, including yeasts with industrially relevant enzymes. Full article

The objective of this study was the evaluation of fungal solid-state fermentation (SSF) for the production of alginate lyase and extraction of uronic acids from Sargassum sp. For this purpose, the fungi Trichoderma asperellum, Aspergillus oryzae, and Rhizopus oryzae were applied (alone or combined) to Sargassum sp. biomass through SSF (10⁷ spores g_biomass⁻¹, 30 °C, and 7 days of treatment). In general, individual SSF with all three fungi degraded the biomass, achieving a marked synergy in the production of cellulase, laminarinase, and alginate lyase activities (especially for the last one). Trichoderma was the most efficient species in producing laminarinase, whereas Rhizophus was the best option for producing alginate lyase. However, when dual combinations were tested, the maximal values of alginate lyase activities were reached (13.4 ± 0.2 IU g_biomass⁻¹ for Aspergillus oryzae and Rhizopus oryzae). Remarkably, uronic acids were the main monomeric units from algal biomass solubilization, achieving a maximum yield of 14.4 mg_uronic g_biomass⁻¹, with the A + R condition being a feasible, eco-friendly alternative to chemical extraction of this monomer. Additionally, the application of all the fungal pretreatments drastically decreased the total phenolic content (TPC) in the biomass from 369 mg L⁻¹ to values around 44–84 mg L⁻¹, minimizing the inhibition for possible subsequent biological processes in which the residual solid can be used. Full article

Stipagrostis pennata is an important plant in desert ecosystems. Its seed-endophytic bacteria may play a critical role in plant growth and environmental adaptation processes. This study systematically analyzed the community composition and potential plant growth-promoting (PGP) functions of seed-endophytic bacteria associated with S. pennata. The results showed that while the overall diversity of bacterial communities from different sampling sites was similar, significant differences were observed in specific functional genes and species abundances. Nine endophytic bacterial strains were isolated from the seeds, among which Bacillus altitudinis strain L7 exhibited phosphorus solubilizing capabilities, nitrogen fixing, IAA production, siderophore generation, and multi-hydrolytic enzyme activities. Additionally, the genomic sequencing of L7 revealed the key genes involved in plant growth promotion and environmental adaptation, including Na⁺ efflux systems, K⁺ transport systems, compatible solute synthesis genes, and the gene clusters associated with nitrogen metabolism, IAA synthesis, phosphate solubilization, and siderophore synthesis. Strain L7 exhibits salt and osmotic stress tolerance while promoting plant growth, providing a promising candidate for desert microbial resource utilization and plant biostimulant development. Full article

Plant subtilases, as hydrolytic enzymes, contribute to certain plant stress response pathways by cleaving precursor proteins into active peptides or through other less well-characterized mechanisms. Phytaspases represent a specific subgroup of subtilases, and their participation in rapid stress responses, particularly to herbivory attacks and drought, is already well established, in contrast to their poorly understood role in long-term responses. This study investigated the involvement of phytaspase NbSBT1.9-2 in the long-term stress responses of Nicotiana benthamiana. Plants were subjected to either mild to severe mechanical wounding or drought stress, followed by the detection of phytaspase activity and gene expression in the leaf tissue. The results revealed a distinct involvement of phytaspase in the wounding response, showing increased activity and upregulated expression correlated with the extent and recurrence of wounding. In contrast, no significant change in phytaspase activity was observed in the leaves under drought, alongside salinity and heat stress conditions. Consequently, phytaspase association with the long-term response to mechanical injury was demonstrated using N. benthamiana as a model organism. Full article

Anaerobic acidogenic fermentation presents a promising approach for sustainable carbon emission mitigation in livestock waste management, addressing critical environmental challenges in agriculture. This study systematically investigated the synergistic effects of composting-assisted pretreatment coupled with micro-aeration and methanogenesis suppression to enhance volatile fatty acid (VFA) production from swine manure supplemented with wheat straw, valorizing agricultural waste while reducing greenhouse gas emissions. The experimental protocol involved sequential optimization of pretreatment conditions (12 h composting followed by 10 min thermal pretreatment at 85 °C), operational parameters (300 mL micro-aeration and 30 mmol/L 2-bromoethanesulfonate (BES) supplementation), and their synergistic integration. The combined strategy achieved peak VFA production (5895.92 mg/L, p < 0.05), with butyric acid constituting the dominant fraction (2004.42 mg/L, p < 0.05). Enzymatic analysis demonstrated significantly higher activities of key hydrolytic enzymes (protease, α-glucosidase) and acidogenic enzymes (butyrate kinase, acetate kinase) in the synergistic treatment group compared to individual BES-supplemented or micro-aeration-only groups (p < 0.05). This integrated approach provides a technically feasible and environmentally sustainable pathway for circular resource recovery, contributing to low-carbon agriculture and waste-to-value conversion. Full article

Plant growth-promoting rhizobacteria (PGPR) are eco-friendly and sustainable options for agrochemicals, particularly for enhancing crop productivity under stress conditions. The present research aims to isolate and characterize native PGPR from tomato rhizospheric soil and to evaluate their effectiveness as a dose-dependent response to enhance the growth of tomato seedlings. Out of 112 isolates, 10 bacterial strains were selected based on key PGPR traits, including indole-3-acetic acid (IAA), ammonia production, hydrogen cyanide (HCN), exopolysaccharide (EPS) synthesis, hydrolytic enzyme activity, potassium solubilization, antifungal activity against Fusarium oxysporum, and tolerance to pH and heat stress. Molecular identification via 16S rRNA gene sequencing confirmed that these isolates belong to the genera Serratia and Enterobacter. S. marcescens So-1 and Enterobacter sp. So-12 produced the highest levels of IAA (2.6–24.1 µg/mL). In vitro tomato seed germination tests using bacterial suspensions at three concentrations (10⁶, 10⁷, and 10⁸ CFU/mL) showed dose-dependent improvements, with T1 increasing germination up to 108.3% compared to the control. In polyhouse trials using cocopeat formulations, seedling growth improved noticeably. T2 increased the root length (28.3 ± 2.98 cm) by over 1560%, and the shoot length (35.7 ± 0.57 cm) increased by 55% against the control, whose root length is 1.7 ± 0.47. The chlorophyll amount of the treated leaves further showed significant results over the control. Collectively, these findings suggest that using native PGPR in a dose-dependent way can help tomato seedlings grow better and promote more sustainable crop production. Full article

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the virus responsible for COVID-19, remains a major global health threat. The virus enters host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor. Several small-molecule antiviral drugs, including molnupiravir, favipiravir, remdesivir, and nirmatrelvir have been shown to inhibit SARS-CoV-2 replication and are approved for treating SARS-CoV-2 infections. Nirmatrelvir inhibits the viral main protease (M^pro), a key enzyme for processing polyproteins in viral replication. In contrast, molnupiravir, favipiravir, and remdesivir are prodrugs that target RNA-dependent RNA polymerase (RdRp), which is crucial for genome replication and subgenomic RNA production. However, undergoing extensive metabolism profoundly impacts their therapeutic effects. Carboxylesterases (CES) are a family of enzymes that play an essential role in the metabolism of many drugs, especially prodrugs that require activation through hydrolysis. Molnupiravir is activated by carboxylesterase-2 (CES2), while remdesivir is hydrolytically activated by CES1 but inhibits CES2. Nirmatrelvir and remdesivir are oxidized by the same cytochrome P450 (CYP) enzyme. Additionally, various transporters are involved in the uptake or efflux of these drugs and/or their metabolites. It is well established that drug-metabolizing enzymes and transporters are differentially expressed depending on the cell type, and these genes exhibit significant polymorphisms. In this review, we examine how CES-related cellular and genetic factors influence the therapeutic activities of these widely used COVID-19 medications. This article highlights implications for improving product design, targeted inhibition, and personalized medicine by exploring genetic variations and their impact on drug metabolism and efficacy. Full article

Fluorinated xenobiotics, such as per- and polyfluoroalkyl substances (PFAS), fluorinated pesticides, and pharmaceuticals, are extensively used across industries, but their extreme persistence, driven by the high carbon–fluorine (C–F) bond dissociation energy (~485 kJ/mol), poses serious environmental and health risks. These compounds have been detected in water, soil, and biota at concentrations from ng/L to µg/L, leading to widespread contamination and bioaccumulation. Traditional remediation approaches are often costly (e.g., EUR >100/m³ for advanced oxidation), energy-intensive, and rarely achieve complete degradation. In contrast, microbial defluorination offers a low-energy, sustainable alternative that functions under mild conditions. Microorganisms cleave C–F bonds through reductive, hydrolytic, and oxidative pathways, mediated by enzymatic and non-enzymatic mechanisms. Factors including electron donor availability and oxygen levels critically influence microbial defluorination efficiency. Microbial taxa, including bacteria, fungi, algae, and syntrophic consortia, exhibit varying defluorination capabilities. Metagenomic and microbial ecology studies continue to reveal novel defluorinating organisms and metabolic pathways. Key enzymes, such as fluoroacetate dehalogenases, cytochrome P450 monooxygenases, reductive dehalogenases, peroxidases, and laccases, have been characterised, with structural and mechanistic insights enhancing the understanding of their catalytic functions. Enzyme engineering and synthetic biology tools now enable the optimisation of these enzymes, and the design of microbial systems tailored for fluorinated compound degradation. Despite these advances, challenges remain in improving enzyme efficiency, broadening substrate specificity, and overcoming physiological constraints. This review emphasises the emerging promise of microbial defluorination as a transformative and green solution, uniquely integrating recent multidisciplinary findings to accelerate the development of sustainable microbial defluorination strategies for effective remediation of fluorinated xenobiotics. Full article

The purpose of this study was to investigate the growth-promoting effects of four rhizobacterial isolates (RS60, RS65, RS46, and RP6) isolated from the tomato rhizosphere. These isolates were screened for key plant growth-promoting rhizobacteria (PGPR) mechanisms, including ammonia production, nitrogen fixation, phosphate solubilization, indole-3-acetic acid (IAA) production, and siderophore synthesis. Their potential to enhance seed germination and tomato plant growth was investigated in controlled and greenhouse conditions. Four isolates exhibited multiple PGPR attributes, notably IAA and ammonia production as well as phosphate solubilization. The results revealed that these strains significantly enhanced tomato seed germination and shoot growth in vitro, with RS65 showing the highest germination rate (70%). However, no significant differences in early seedling responses were observed under greenhouse conditions when compared to the control. Thirty days after inoculation, greenhouse results revealed that the four studied strains significantly increased growth metrics including shoot length, number of leaves, collar diameter, and dry weight. The isolate RP6 showed a significant effect on the growth of the plant, with an average shoot length of 34.40 cm and nine leaves per plant. In vitro antagonism assays demonstrated that isolates RS60, RS65, and RP6 effectively inhibited the growth of Botrytis cinerea, Alternaria alternata, and Oidium lycopersici, with inhibition rates exceeding 65%. These antagonistic activities were linked to the production of hydrolytic enzymes (chitinase, cellulase, pectinase, protease), siderophores, and hydrogen cyanide (HCN). Molecular identification through 16S rRNA gene sequencing confirmed the isolates as Bacillus cereus (RS60), Bacillus pumilus (RS46), Bacillus amyloliquefaciens (RP6), and Bacillus velezensis (RS65), each showing over 97% sequence similarity with reference strains. These findings underscore the potential of the selected Bacillus spp. as promising biofertilizers and biocontrol agents for sustainable tomato cultivation and support their inclusion in integrated disease and nutrient management strategies. Full article

Microorganisms from saline environments have garnered significant interest due to their unique adaptations, which enable them to thrive under high-salt conditions and synthesize valuable biomolecules. This study investigates the biosynthesis of biomolecules, such as extracellular hydrolytic enzymes, biosurfactants, and carotenoid pigments, by four newly halotolerant bacterial strains isolated from saline environments in the Băicoi (soil, water) and Curmătura (mud) area (Prahova County, Romania). Isolation was performed on two selective culture media with different NaCl concentrations (1.7 M, 3.4 M). Based on their phenotypic and molecular characteristics, the four halotolerant bacteria were identified as Halomonas elongata SB8, Bacillus altitudinis CN6, Planococcus rifietoensis CN8, and Halomonas stenophila IB5. The two bacterial strains from the Halomonas genus exhibited growth in MH medium containing elevated NaCl concentrations (0–5 M), in contrast to the other two strains from Bacillus (0–2 M) and Planococcus (0–3 M). The growth of these bacteria under different salinity conditions, hydrocarbon tolerance, and biomolecule production were assessed through biochemical assays, spectrophotometry, and high-performance thin-layer chromatography. The antimicrobial properties of biosurfactants and carotenoids produced by H. elongata SB8, B. altitudinis CN6, P. rifietoensis CN8, and H. stenophila IB5 were evaluated against four reference pathogenic microorganisms from the genera Escherichia, Pseudomonas, Staphylococcus, and Candida. H. elongata SB8 showed the highest hydrocarbon tolerance. B. altitudinis CN6 exhibited multiple hydrolase activities and, along with H. elongata SB8, demonstrated biosurfactant production. P. rifietoensis CN8 produced the highest carotenoid concentration with antifungal and antimicrobial activity. Exploring these organisms opens new pathways for bioremediation, industrial bioprocessing, and sustainable biomolecule production. Full article

An experimental model of acute pulmonary damage was developed based on the intravenous injection of the phospholipase A₂ (PLA₂)-rich venom of Pseudechis papuanus (Papuan black snake) in mice. Venom caused pulmonary edema, with the accumulation of a protein-rich exudate, as observed histologically and by analysis of bronchoalveolar lavage fluid (BALF). In parallel, venom induced an increase in all of the pulmonary mechanical parameters evaluated, without causing major effects in terms of tracheal and bronchial reactivity. These effects were abrogated by incubating the venom with the PLA₂ inhibitor varespladib, indicating that this hydrolytic enzyme is responsible for these alterations. The venom was cytotoxic to endothelial cells in culture, hydrolyzed phospholipids of a pulmonary surfactant, and reduced the activity of angiotensin-converting enzyme in the lungs. The pretreatment of mice with the nitric oxide synthase inhibitor L-NAME reduced the protein concentration in the BALF, whereas no effect was observed when mice were pretreated with inhibitors of cyclooxygenase (COX), tumor necrosis factor-α (TNF-α), bradykinin, or neutrophils. Based on these findings, it is proposed that the rapid pathological effect of this venom in the lungs is mediated by (a) the direct cytotoxicity of venom PLA₂ on cells of the capillary–alveolar barrier, (b) the degradation of surfactant factor by PLA₂, (c) the deleterious action of nitric oxide in pulmonary tissue, and (d) the cytotoxic action of free hemoglobin that accumulates in the lungs as a consequence of venom-induced intravascular hemolysis. Our findings offer clues on the mechanisms of pathophysiological alterations induced by PLA₂s in a variety of pulmonary diseases, including acute respiratory distress syndrome (ARDS). Full article

Our previous study demonstrated that an Escherichia coli heterologous secretion expression system, mediated by superfolder green fluorescent protein (sfGFP) mutants, significantly enhances recombinant lipase yield and reduces large-scale production costs. In this study, we identified mScarlet3, a fast-folding fluorescent protein, as another effective mediator of secretion expression in E. coli. A novel lipolytic enzyme, named LipHu6, was identified through sequence alignment. Secretion expression of LipHu6 was achieved by fusing mScarlet3 to either its N- or C-terminus. The specific activity of mScarlet3-LipHu6 reached 669,151.75 U/mmol, slightly surpassing that of LipHu6 alone (646,682.69 U/mmol) and markedly exceeding that of sfGFP_(-15)-LipHu6 (492,432.39 U/mmol). Notably, N-terminal mScarlet3 fusion had no impact on LipHu6 hydrolytic activity toward short-chain p-nitrophenyl fatty acyl esters (C2–C8). In contrast, mScarlet3-LipHu6 exhibited approximately 1.5- and 1.7-fold increases in hydrolytic activity toward p-nitrophenyl palmitate (p-NPP, C16) and p-nitrophenyl stearate (p-NPS, C18), respectively. In conclusion, this study establishes a novel E. coli heterologous secretion expression system mediated by mScarlet3, offering a highly efficient and cost-effective strategy for the large-scale production of lipolytic enzymes. Full article