Bioinformatics analysis of extracellular glycosyl hydrolases mined from the genome of Halophilic Meridianimaribacter sp. CL38.

Production of Some Extracellular Hydrolases by Halophilic Bacteria Isolated from Mangrove Soil in Sumberkima Village, Bali, Indonesia

Hydrolases are enzymes with broad industrial applications across the food, pharmaceutical, textile, detergent, and paper sectors. For commercial use, these enzymes are primarily sourced from microorganisms. Halophilic bacteria, which thrive in high-salinity environments, represent a promising yet underutilized source of novel hydrolases. This study aimed to isolate and screen halophilic bacteria from mangrove soil in Sumberkima Village, Buleleng Regency, Bali Province, Indonesia, for their ability to produce extracellular hydrolases. Soil samples were cultivated on Luria-Bertani (LB) media supplemented with 5% and 10% (w/v) NaCl. Putative colonies were isolated and screened for amylase, cellulase, and lipase production using starch, carboxymethyl cellulose, and rhodamine-olive oil agar, respectively. Enzymatic activities were quantified via spectrophotometry, and the most proficient isolates were identified through 16S rRNA gene phylogenetic analysis. The screening yielded several halophilic bacteria with significant extracellular hydrolase activity. The most proficient isolates identified were: amylase-producing Vibrio xiamenensis SKMG1(4) (0.44 U/mL), cellulase-producing Vibrio hepatarius SKMG1(3) (0.36 U/mL), and lipase-producing Salinivibrio kushneri SKMG2(5) (21.6 U/mL). Phylogenetic analysis confirmed the close taxonomic relationship of these isolates to their respective type strains. This study represents the first report of extracellular hydrolase production from these three halophilic bacterial species, highlighting their potential for specialized industrial applications.

Genomic and structural insights into the high-efficiency poly(3-hydroxybutyrate) biodegradation in Terrabacter sp. AAH1

By proposing a putative association between specific genomic features and macroscopic polymer degradation, this study suggests that Terrabacter sp.

Predictive characterization and molecular docking of lignocellulolytic enzymes: comparative analyses of Moroccan fungal species

Lignocellulosic biomass has significant potential as a renewable feedstock for the production of biofuels and bioproducts. However, its structural complexity, particularly the crystalline nature of cellulose and protective lignin matrix, poses considerable challenges for enzymatic degradation. Fungi isolated from diverse lignocellulosic wastes, particularly olive pomace in Morocco, are a significant, yet underutilized resource of lignocellulolytic enzymes with a potential to overcome these challenges. This study investigated the structural and functional properties of lignocellulolytic enzymes derived from 9 filamentous fungi. A total of 80 curated sequences were systematically categorized into cellulases and ligninases. Phylogenetic analysis was conducted on representative endo­glucanases, β-glucosidases, and laccases to assess their diversity. Physicochemical parameters, secon­dary structure content, and thermostability indices were determined using ExPASy ProtParam and SOPMA. Homology models were generated with SWISS-MODEL and validated through PROCHECK, ERRAT, and ProSA. Molecular docking with AutoDock was used to evaluate the interactions of β-glucosidase with cellobiose. Phylogenetic analysis revealed high evolutionary diversity among the examined species. Seve­ral enzymes showed favorable aliphatic indices and GRAVY scores, suggesting thermostability and hydrophilicity. β-Glucosidase from Fusarium equiseti showed the strongest predicted binding energy to cellobiose (–5.32 kcal/mol), with hydrogen bonding mediated by key residues, including Asp88, Arg94, Lys185, Gln197, Asp276, and Gln278, at optimal distances (1.95–2.58 Å). This integrative in silico study highlights the predictive potential of Moroccan fungal β-glucosidases, particularly from F. equiseti, for future applications in lignocellulose bioconversion.

Characterization of a Novel GH3 β-Glucosidase with Alkali-Tolerant and Halophilic Properties from Pontixanthobacter luteolus SW-109.

Local enrichment of acidic residues on the PlGH3 surface could generate a negative electrostatic potential, which enables adaptation to high-salt and alkaline environments, thereby sustaining the enzyme's catalytic activity under such extreme conditions.

Deciphering the structural–functional dynamics of glucosyltransferases from novel Apilactobacillus isolates through in silico analysis

Experimental, Genomic, and Structural Evidence Supporting Putative PET‐Hydrolases in Thermophilic Bacteria Isolated From Hot Springs in Cajamarca, Peru

ABSTRACT Polyethylene terephthalate (PET) waste represents a major environmental challenge due to limited recycling solutions. Thermophilic bacteria from geothermal environments harbor diverse enzymatic machinery adapted to extreme conditions, offering promising biocatalysts for plastic degradation; however, biological resources from Peru and other South American countries remain scarce. We characterized four bacterial strains isolated from two geothermal sites in Cajamarca, Peru, screened for PET hydrolysis at 50°C. Whole‐genome sequencing using hybrid assembly achieved near‐complete circular genomes. GTDB‐Tk classification identified three species: Neobacillus thermocopriae (strain 19A), Bacillus licheniformis (strains 16P and BI2), and Brevibacillus agri (strain BI8). Quantitative assays revealed that strain 16P achieved the highest mass loss (0.598%), followed by strain BI8 (0.449%). ATR‐FTIR analysis of the incubated sheets showed a significant reduction of the ester carbonyl index in strains 16P, 19A, and BI8 relative to both non‐incubated PET and an abiotic control, whereas strain BI2 did not differ from the controls, indicating preferential modification of ester bonds at the sheet surface. Genome mining and structure‐based homology searches identified multiple candidate enzymes similar to validated PETases and carboxylesterases, including PETase46‐like homologs in strains BI8 and 16P and a terephthalate‐active carboxylesterase homolog in strain 16P. Molecular docking supported the conservation of catalytic geometry and substrate‐binding sites in these candidates. This work represents one of the first systematic genomic and structural characterizations of putative PET‐hydrolases in Peruvian geothermal bacteria, expanding knowledge of extremophile diversity and advancing thermostable enzymes for sustainable plastic waste management.