Fungi associated with basal stem rot-infected oil palm trees inhabit lignocellulose-rich environments and may provide robust cellulolytic enzymes. This study optimized endoglucanase production by Schizophyllum commune MA1, purified and characterized the enzyme, and preliminarily assessed a partially purified preparation against chemically pretreated agricultural residues. Taguchi screening followed by a central composite design within response surface methodology (RSM) increased carboxymethyl cellulase (CMCase) activity by 150%, from 0.60 to 1.50 U/mL. Ammonium sulfate precipitation and chromatographic purification yielded a 36.8-kDa endoglucanase with 24.4-fold purification and a specific activity of 1,181 U/mg. The purified enzyme showed maximal activity at pH 2.5 and 60 °C, retained full activity after 24 h at pH 2.5, and remained approximately 100% active at 50 °C for one month under the tested buffer conditions. The partially purified preparation hydrolyzed all tested residues; rice straw produced the highest reducing sugar concentration (1.95 g/L after 168 h), and scanning electron microscopy revealed marked fiber disruption after enzymatic treatment. This combination of strong acid activity, prolonged thermal stability, and biomass-hydrolyzing capability expands the known functional diversity of S. commune cellulases and provides proof-of-concept support for acidic, extended-duration lignocellulosic saccharification.

Biofilm-associated bacterial infections pose a significant challenge in clinical settings due to their persistence and reduced susceptibility to current antimicrobials, underscoring the need for novel antibiofilm agents. This study aimed to evaluate the antibacterial and antibiofilm activities of cell-free extracts from marine Streptomyces sp. using integrated in vitro and in silico approaches. Initial antibacterial screening by agar well diffusion assay identified VITNABS17 as the most active isolate, exhibiting a broad antibacterial spectrum against the tested bacterial pathogens. Evaluation of biofilm formation by tube method revealed K. pneumoniae as the strongest biofilm-forming pathogen. The ethyl acetate extract of VITNABS17 reduced K. pneumoniae biofilm biomass by 66.2 ± 0.22% at 20 mg/mL, while the minimum biofilm inhibitory concentration (MBIC) was 1 mg/mL, corresponding to 55.50% inhibition. GC-MS analysis revealed a diverse metabolite profile, with diethyl phthalate identified as the most abundant compound. Molecular docking predicted binding affinities of -6.0 kcal/mol for MrkA and -4.4 kcal/mol for LuxS, indicating potential interactions of diethyl phthalate with biofilm-associated protein targets. The potential isolate was identified as Streptomyces sp. VITNABS17 by 16S rRNA gene sequencing. Overall, these findings provide preliminary evidence for the antibiofilm potential of VITNABS17 and warrant further investigation into the identification and characterization of its active metabolites.

This study presents the biosynthesis of a ZnO-TiO2 nanocomposite using an aqueous extract of the green macroalga Chaetomorpha crassa for sunscreen application. Chaetomorpha crassa is a potential source of antioxidant and anti-inflammatory compounds. GC-MS analysis revealed bioactive compounds and phytochemical screening confirmed alkaloids and flavonoids. The extract showed a Total Phenolic Content of 5.26 ± 1.70 mg GAE/g and Total Flavonoid Content of 8.51 ± 0.75 mg QE/g, which may contribute to its antioxidant properties. The nanocomposite formed a grey suspension and was calcined to fine powder. UV-Visible spectroscopy showed a peak at 374.0 nm. FTIR identified functional groups potentially involved in nanoparticle formation, while XRD confirmed crystalline structure and phase purity. DLS showed a hydrodynamic diameter of 61.6 nm (PDI 0.43), SEM revealed rough spherical morphology and EDS confirmed Zn, Ti and O. The nanocomposite showed antioxidant (DPPH IC50 = 562.7 µg/mL) and anti-inflammatory (Egg albumin IC50 = 676.1 µg/mL) activities, while extract and nanocomposite exhibited antibacterial potential. Among four formulations, F1 was selected for its UVB protection (307.1 nm) and antibacterial activity, with an SPF of 17.35 ± 0.13. These findings suggest the potential of algae-mediated ZnO-TiO2 nanocomposites for further evaluation in cosmetic sunscreen applications.

The accumulation of lignocellulosic waste from agricultural and industrial activities poses significant environmental challenges while offering a renewable resource for sustainable biorefineries. Immobilization of lignin-degrading enzymes on functionalized nanomaterials enhances enzyme stability, catalytic efficiency, reusability, and recovery, thereby improving lignocellulosic biomass conversion into fermentable sugars, biofuels, and value-added chemicals. Various nanocarriers, including magnetic nanoparticles, mesoporous silica, carbon nanomaterials, and metal-organic frameworks, provide efficient enzyme support through enhanced surface area and tailored immobilization strategies. Advanced approaches, such as stimulus-responsive nanocarriers and multi-enzyme co-immobilization, further improve catalytic performance and conversion efficiency. Collectively, nanomaterial-assisted enzyme immobilization offers an effective and sustainable strategy for lignocellulosic bioconversion, supporting waste valorization and the development of a circular bioeconomy.

Acetyl esterases play an important role in the deacetylation of hemicellulose. This study aimed to identify and characterize a novel carbohydrate esterase family 16 (CE16) acetyl esterase from the saprophytic fungus Stropharia rugosoannulata and evaluate its potential for enhancing the enzymatic depolymerization of natural lignocellulosic substrates under mild conditions. A putative CE16 family gene was identified through genomic mining and heterologously expressed in Escherichia coli. The recombinant enzyme, SrAEA, was purified and biochemically characterized. The synergistic effect of SrAEA with xylanase was evaluated on beechwood powder, corncob powder, and rice bran. SrAEA exhibited optimal catalytic activity at 20 °C and pH 7.0, defining it as a cold-adapted enzyme. Structural analysis showed that it possesses a non-canonical Ser-His-Asn catalytic triad and a conserved SGNH-hydrolase fold. The enzyme exhibited the highest catalytic efficiency toward the short-chain substrate 4-methylumbelliferyl acetate, with no detectable activity on longer-chain substrates. Sequential treatment with SrAEA and xylanase increased reducing-sugar release in a substrate-dependent manner. These findings identify SrAEA as a fungal CE16 acetyl esterase with activity at 20 °C and show that its sequential use with xylanase can increase reducing-sugar release under the tested conditions. Its process utility and energy requirements remain to be evaluated.

The industrial demand for proteases necessitates the development of cost-effective and sustainable production processes. Leveraging insect biomass, such as Hermetia illucens meal, aligns with circular bioeconomy principles and offers a promising alternative to fungal fermentation substrates. This study reports, for the first time, protease production by filamentous fungi isolated from the Caatinga-Cerrado ecotone using Hermetia illucens meal as a substrate for solid-state fermentation (SSF). T. koningiopsis UFPIT03 showed the highest activity (88.24 U/mL). A 2[3] factorial design identified moisture (30%) as a key factor for this activity. Purification via salting-out and ion-exchange chromatography achieved a 15-fold increase in purity (46.13 kDa). The enzyme exhibited optimal activity at pH 7.0 and 50 °C and was characterized as a trypsin-like serine protease. Kinetic analysis revealed a high substrate affinity, whereas thermodynamic parameters demonstrated high conformational stability and a non-spontaneous denaturation process. Furthermore, the protease exhibited remarkable compatibility with various commercial detergents, retaining substantial residual activity. These results highlight the potential of T. koningiopsis to produce robust neutral proteases using insect biomass. The stability and resilience of the enzyme in detergent formulations validate its suitability for biotechnological applications, offering a viable path for the valorization of alternative resources within the global bioeconomy.

Immobilization of lipases in metal-organic frameworks offers a potential route for developing robust biocatalysts for ester synthesis, but achieving efficient enzyme incorporation within structurally favorable hosts remains challenging. Here, we report a biomimetic mineralization strategy based on layered ZIF-8 for immobilization of Candida antarctica lipase B (CALB) and evaluate the resulting biocatalyst for the synthesis of isosorbide dihexanoate (SDH). Under optimized immobilization conditions, namely a CALB dosage of 1 mL, a Zn[2+]/2-methylimidazole molar ratio of 1:3, and a mineralization time of 6 h, CALB@mZIF-8 exhibited a protein loading of 201.50 mg/g and an activity of 36.71 U/g. The protein loading was higher than that obtained by conventional adsorption-based immobilization using ZIF-8. Applied to SDH synthesis in a 10 mL reaction system containing n-hexane (10%, v/v) as co-solvent, 0.4 g CALB@mZIF-8, an isosorbide-to-hexanoic acid molar ratio of 1:6, agitation at 150 rpm and 40 °C, the SDH yield reached 65.03%. Compared with free CALB, the immobilized biocatalyst exhibited enhanced operational stability and improved tolerance toward different reaction environments. These results demonstrate that layered ZIF-8 generated through biomimetic mineralization provides a tunable platform for lipase immobilization and represents a promising strategy for the synthesis of sterically hindered bio-based esters.

Nitrogen limitation suppresses growth and target metabolite synthesis of industrial yeast, and the key transcription factor coordinating carbon-nitrogen balance in Candida glycerinogenes remains unclear. This work identified CgGCN4 as the core effector of nitrogen starvation response: screen nitrogen-starvation responsive transcription factor in C. glycerinogenes; characterize physiological function via overexpression and antisense repression in glycerol-producing yeast; test cross-species function by heterologous expression in S. cerevisiae for ethanol fermentation application. qRT-PCR reveals nitrogen starvation activates three nutrient-sensing pathways, with CgGCN4 showing the highest transcript level (4.2). At 84 h fermentation, CgGCN4-OE consumes 250.2 g/L glucose, yields 122.6 g/L glycerol and reaches OD600 of 45.6, outperforming wild type. Transcriptomics demonstrates CgGCN4 co-upregulates glycolysis, TCA and amino acid synthesis to balance C/N metabolism. Its conserved function is validated in Saccharomyces cerevisiae. In 5 L fed-batch culture, engineered Sc-BNA-MG produces 67.7 g/L ethanol (10.1% higher than control), with intracellular NAD(H) pool rising by 27.5% at 6 h. CgGCN4 serves as a cross-species regulatory hub mitigating low-nitrogen stress, a promising target for yeast factory engineering.

This review highlights the pivotal role of Plant Growth Promoting Rhizobacteria (PGPR) in association with nanotechnology for enhancing plant growth and health. It narratively discusses diverse PGPR groups and genera, outlining their direct mechanisms such as phosphate solubilization, nitrogen fixation, ACC deaminase activity, hydrogen cyanide production, and siderophore production for iron chelation as well as indirect mechanisms through induced systemic resistance (ISR) and systemic acquired resistance (SAR). The application of PGPR as single inoculants and in consortia, together with omics-based approaches, is examined to demonstrate their versatility in sustainable crop improvement. PGPR interactions with host plants, contributions to soil protection, and conditioning are also addressed. Despite their multifaceted benefits, limitations such as loss during aerial application or environmental stress remain challenges. Emerging nanotechnology-based delivery systems offer promising solutions by enabling controlled release of PGPR and their bioactive compounds, thereby targeting specific tissues and enhancing resilience under variable conditions. Collectively, this review underscores PGPR- mediated green nanotechnological strategies as eco- friendly alternatives to hazardous chemical inputs, advancing climate-resilient and sustainable agriculture.

β-fructofuranosidases (FFases) catalyze the hydrolysis of sucrose, producing commercially valuable products such as invert sugar. However, the use of enzymes in industry faces limitations due to operational instability. Immobilization emerges as an alternative to reduce these instabilities, improving stability and enabling reuse. The objective of this study was to immobilize the FFase from A. tamarii URM4634 onto Fe3O4 magnetic nanoparticles coated with chitosan, to biochemically characterize it, study its kinetic and thermodynamic parameters, and apply it in sucrose hydrolysis. Immobilization was carried out according to a full 2[2] factorial design with variations in glutaraldehyde concentration and contact time. A high activity yield was obtained (94.45%), which exhibited optimal activity at 60 °C and pH 7.0, maintaining full catalytic activity over 8 consecutive reuse cycles. Immobilization significantly increased thermostability at 50 °C, evidenced by the increase in thermal denaturation activation energy (E*d = 322.16 kJ mol[-1]) and a stabilization factor of 1.92 relative to the free enzyme. The application of immobilized FFase in invert sugar synthesis achieved a maximum sucrose conversion of 49.39%. These results, combined with the ease of magnetic separation from the reaction medium, highlight the biotechnological potential of the immobilized enzyme for the industrial production of invert sugar.

Agro-industrial-residues, such as potato peel waste (PPW), constitute a substantial portion of the waste stream and offer significant opportunities for valorization within circular bioeconomy frameworks. In this study, a laboratory-scale solid-state fermentation (SSF) process for biosurfactant production using fresh or dried PPW as renewable substrates was optimized with Saccharomyces cerevisiae BY4742. A Box-Behnken design was implemented to optimize peel amount, initial pH, and incubation time, targeting enhanced surface tension reduction. Under optimized conditions (10 g fresh PPW, pH 5.25, 5[th] day), the biosurfactant reduced surface tension to 30.12 ± 0.32 mN/m and demonstrated a high emulsification index (51.35 ± 0.49%), low critical micelle concentration (1.1 ± 0.09 mg/mL), strong oil spreading activity (6.3 ± 0.05 cm), and positive drop collapse results. Partial structural characterization by FTIR,[1]H-NMR and TGA/DTG was consistent with a heterogeneous surface-active biopolymeric fraction, supporting its robust functional properties. The obtained biosurfactant maintained remarkable stability across wide ranges of pH, temperature, and salinity, while achieving an oil removal efficiency of 91.37 ± 0.89%, indicating its strong potential for bioremediation applications. Notably, the SSF platform enabled the simultaneous production of a surface-active fraction and extracellular amylase activity, highlighting the potential of PPW-based SSF as a resource-efficient approach for producing value-added bioproducts.

In this work, fucoxanthin (Tc-fuco) was isolated from the crude extract of T. conoides (Tc-cru), and evaluated its antioxidant, antibacterial, and toxicity studies for biomedical applications. Characterized using TLC, UV-Vis, FTIR, HPLC, LCMS and NMR analyses confirmed the pigment nature and functional groups, with a yield of 0.2068 mg/g FW. The Tc-cru performed less antibacterial activity than the isolated Tc-fuco; inhibition zones (mm) for Tc-cru were 6 (P. aeruginosa), 6.2 (S. aureus), 5 (E. faecalis), 5.5 (E. coli), whereas Tc-fuco produced larger zones (mm) of 9 (P. aeruginosa), 7.5 (S. aureus), 8 (E. faecalis), and 8.5 (E. coli), respectively. In DPPH, and H2O2 assays, Tc-fuco demonstrated potent antioxidant effects with IC50 values of 44.61 and 43.03 µg/mL, respectively. This outperformed the crude extract (Tc-cru), which exhibited IC50 values of 60.36 and 75.18 µg/mL, respectively. Light and confocal microscopy images displayed a dose dependent reduction in biofilm formation relative to control groups. Furthermore, the toxicity of Tc-cru and Tc-fuco in A. salina was assessed following 24 hours exposure. Biochemical responses evaluated at 48 hours, confirmed the nontoxicity and sustainable development of tested doses. These findings suggest that the isolated fucoxanthin might be utilized in production of new antibacterial drugs.

This study evaluated Natrix[®] Q anion membrane chromatography for the purification of Streptococcus pneumoniae serotype 5 capsular polysaccharide (CPS) as an alternative to conventional organic solvent-based purification and bead-based ion-exchange chromatography. The purification process was optimized and characterized using a Design of Experiments (DoE) approach to establish a robust operating space for key process parameters. Under the optimized conditions, residual DNA was reduced to below 2%, while CPS recovery remained above 80%. The membrane process achieved a loading capacity of 45-60 mg CPS/mL membrane, approximately 4-6-fold higher than that of conventional anion-exchange resins (<10mg/mL), and operated at a residence time of approximately 6s, substantially shorter than the approximately 5 min typically required for bead-based ion-exchange chromatography. The CPS recovery was also higher than the previously reported range of 50%-73%. Scale-up studies further demonstrated that the optimized process could be successfully transferred to scale production. Product quality was evaluated by double immunodiffusion, proton nuclear magnetic resonance ([1]H-NMR) spectroscopy, and relevant biochemical and physicochemical assays. The CPS purified by membrane chromatography met the predefined quality requirements. These results demonstrate that Natrix[®] Q anion membrane chromatography provides an efficient, high-throughput, and scalable approach for the purification of serotype 5 pneumococcal CPS and has potential for application in large-scale pneumococcal polysaccharide vaccine manufacturing.

Microalgae are prolific producers of volatile organic compounds (VOCs) that play important roles in atmospheric chemistry, aquatic ecosystem dynamics, and water quality, particularly through the generation of off-flavours and odors. Despite their ecological relevance and growing biotechnological interest, microalgal VOCs remain comparatively underexplored. These low-molecular-weight metabolites encompass a broad range of chemical classes, including terpenoids, sulfur-containing compounds, benzenes, furans, alkanes, alcohols, ketones, aldehydes, and esters. Knowledge of their chemical diversity, biosynthetic pathways, allelopathic effects, and other ecological functions is still not fully reviewed. This review synthesizes current understanding of microalgal VOCs, emphasizing how morphology, physiology, ecological niche, and genetic variability influence VOCs production. Commonly reported VOCs such as geosmin, methylisoborneol, β-cyclocitral, and 2-pentylfuran are discussed with respect to their occurrence, chemistry, ecological roles, regulation by biotic and abiotic factors, and impacts. Despite their diverse ecological and biochemical roles, limited elucidation of their biosynthetic mechanisms also highlighted. Microalgal VOCs exhibit diverse bioactivities, including antibacterial, antifungal, insecticidal, antioxidant, antiviral, and antiprotozoal properties, underscoring their potential for biotechnological and industrial applications. Advances in analytical approaches, particularly gas chromatography-mass spectrometry and electronic nose technologies, have significantly improved VOCs detection and profiling. This review identifies critical knowledge gaps and underscores the need for integrative studies to unravel the diversity, chemical structures, biosynthetic pathways, and ecological significance of microalgal VOCs, thereby enabling theirsustainable exploitation and facilitating their industrial applications.

Chitinases are gaining importance as biocatalysts for environmentally friendly food preservation and biocontrol. The present study reports on the purification and biochemical characterization of a chitinase from Bacillus cereus V5331 and its anti-yeast activity in grape juice. The enzyme was purified by Sephadex G-100, leading to 10.3-fold purity and a specific activity of 2951 U mg[-1]. The molecular weight of ∼54 kDa was confirmed by SDS-PAGE and zymogram analysis. The chitinase showed optimum activity at pH 7.0 °C and 37 °C. Substrate specificity tests exhibited highest activity toward swollen chitin. Kinetic analysis also revealed the lowest Km (0.023) and Vmax of 77.5 for swollen chitin, showing good substrate affinity and catalysis. Metal ions, halogens, organic solvents, and essential oils greatly influenced enzyme activity, indicating the enzyme's sensitivity to environmental factors. A high-performance liquid chromatography (HPLC) study showed NAG as the major hydrolysis product of chitin. Purified chitinase was found to be effective in suppressing the growth of Saccharomyces cerevisiae in grape juice, resulting in a ∼5-log decline in viable cell counts. This was followed by a time-dependent rise in NAG release as a marker of increasing cell wall degradation. The obtained results suggest the possible applications of B. cereus V5331 chitinase as a natural biocontrol agent in food preservation systems. Furthermore, the availability of a functionally active enzyme increases its potential for industrial and agricultural applications, such as long-term bioconversion of chitinous waste, and simplifies downstream processing.