Enzyme and Microbial Technology最新文献

{"title":"Leveraging Se-nanoparticle@Candida tropicalis for efficient di-carboxylic acid production and methodological advances in selective product separation","authors":"Pragya Gupta,&nbsp;Prakash C. Sahoo,&nbsp;Srikanth Sandipam,&nbsp;Manoj Kumar,&nbsp;Ravi Prakash Gupta,&nbsp;Rajesh Badhe,&nbsp;Umish Srivastva,&nbsp;Alok Sharma","doi":"10.1016/j.enzmictec.2025.110681","DOIUrl":"10.1016/j.enzmictec.2025.110681","url":null,"abstract":"<div><div>This study investigates a bio-inorganic hybrid of selenium nanoparticles (SeNP@<em>C. tropicalis</em>) with an in-house developed mutant of <em>Candida tropicalis</em> (Castellani) Berkhout for enhanced bioconversion of crude dodecane (C₁₂H₂₆) into di-carboxylic acids (DCAs) under challenging conditions. The presence of <em>SeNP@C. tropicalis</em> improves NAD+ /NADH regeneration by enhancing enzymatic activity, thereby optimizing the metabolic transformation process. The activation of low-reactivity alkanes to DCAs, facilitated by cytochrome P450 monooxygenase, NADPH, and alcohol dehydrogenase (ADH), presents a sustainable approach for biorefineries when paired with effective downstream processing. At a 2 L scale, the SeNP@<em>C. tropicalis</em> hybrid achieved a 40.87 % increase in DCA production compared to the control. High-resolution transmission electron microscopy (HRTEM) confirmed the deposition of well-defined, spherical SeNP@<em>C. tropicalis</em> on the yeast surface, and X-ray diffraction (XRD) spectra validated the crystallinity of the nanoparticles, along with Confocal imaging. For downstream processing, four methods were evaluated, with vacuum distillation followed by crystallization achieving the highest DCA purity (&gt;75 %) and recovery (&gt;84 %). This research highlights the potential of SeNP@<em>C. tropicalis</em> as an effective catalyst for DCA production, offering new opportunities for advancing bioconversion technologies and enhancing the sustainability of biorefineries.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110681"},"PeriodicalIF":3.4,"publicationDate":"2025-05-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144154503","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Nano-azurin peptide as an inducer of innate immune responses","authors":"Nawal E. Al-Hazmi ,&nbsp;Hussam A. Althagafi ,&nbsp;Fahad Alharthi ,&nbsp;Hind Althagafi ,&nbsp;Deema Fallatah ,&nbsp;Jamilah Alshammari ,&nbsp;Deyala M. Naguib","doi":"10.1016/j.enzmictec.2025.110675","DOIUrl":"10.1016/j.enzmictec.2025.110675","url":null,"abstract":"<div><div>Azurin, a redox-active protein derived from <em>Pseudomonas aeruginosa</em>, has demonstrated antimicrobial and anticancer properties. In this study, we evaluated for the first time the immunomodulatory effects of its nanoparticle form (nano-azurin) on key innate immune cells—neutrophils, macrophages, and natural killer (NK) cells. Nano-azurin (0.1–1 µg/mL) significantly enhanced neutrophil-mediated killing of <em>Campylobacter jejuni</em> and <em>Enterococcus faecalis</em>, increasing killing efficiency from baseline values of −15 % and −7 % to −83 % and −76 %, respectively. It also potentiated neutrophil-mediated inhibition of cancer cell proliferation. In macrophages, nano-azurin stimulated phagocytic activity in a dose-dependent manner, with the highest enhancement observed against <em>Bacillus cereus</em> (404.6 % increase at 1 µg/mL). Cytokine analysis revealed that nano-azurin attenuated LPS-induced production of proinflammatory cytokines (TNF-α, IL-1β, IL-6) while markedly increasing anti-inflammatory IL-10, with levels rising up to 441.9 % compared to LPS treatment alone. In NK cells, nano-azurin significantly increased cytotoxicity against multiple cancer cell lines, reaching levels comparable to IL-2 stimulation. Additionally, nano-azurin elevated IFN-γ and TNF-α production, indicating activation of NK-mediated immune responses. These findings demonstrate that nano-azurin enhances antimicrobial and anticancer functions of innate immune cells and modulates cytokine responses, supporting its potential as a novel immunotherapeutic agent.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110675"},"PeriodicalIF":3.4,"publicationDate":"2025-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144154502","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Engineering of ω-transaminase at binding pocket and access tunnel for preparation of (R)-1-phenoxypropan-2-amine","authors":"Jinmei Zhu,&nbsp;Ximeng Liu,&nbsp;Dan Zhang,&nbsp;Jiequn Wu","doi":"10.1016/j.enzmictec.2025.110680","DOIUrl":"10.1016/j.enzmictec.2025.110680","url":null,"abstract":"<div><div>Transaminase-catalyzed amination of prochiral ketones is regarded as a promising route for optically active amines production. These chiral amines serve as key building blocks in the synthesis of agrochemicals and pharmaceuticals. However, the limited substrate scope and substrate/(co)product inhibition have significantly hindered the industrial-scale implementation of transaminase-catalyzed processes. Engineering of TAs at binding sites is an efficient strategy to expand the capacity of binding pocket, thereby improving the catalytic efficiency. Furthermore, modification of access tunnel is crucial for adjusting the transfer efficiency of ligand. In this endeavor, we engineered an ω-TA from <em>Nocardioides sp.</em> CER19(<em>Ns</em>TA) at binding sites and access tunnel, and applied the mutants for enantioselective synthesis of (<em>R</em>)-1-phenoxypropan-2-amine. Mutation at residues H62 and Y122 increased catalytic activity of the TA towards 1-phenoxyacetone, the optimal mutants <em>Ns</em>TA_H62A and <em>Ns</em>TA_Y122A with improved enzyme activity was obtained, which was 2.0 and 1.5-fold higher than that of the wild-type <em>Ns</em>TA respectively. This allowed completely conversion of 5 mM 1-phenoxyacetone to (<em>R</em>)-1-phenoxypropan-2-amine at 4 h and &gt; 99 % ee (in comparison to 66 % convesion with the wild-type <em>Ns</em>TA). Molecular dynamic simulation suggested improved flexibility of NsTA_H62A, which may result in eliminating of substrate inhibition. While mutant <em>Ns</em>TA_D7 (with deletion of 7 amino acids at N-terminal) exhibited about 1.6-fold increase of conversion. Tunnel analysis suggested that reshaping of the tunnel entrance may alter the shape and size of the tunnel, which might promote the release of the products. These results of our study lay the foundation for enantioselective synthesis of (<em>R</em>)-1-phenoxypropan-2-amine and provide a promising engineering strategy to enhance the activity of TAs and overcome substrate/(co)product inhibition of ω-TA towards bulky substrates.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110680"},"PeriodicalIF":3.4,"publicationDate":"2025-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144134221","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Probiotic potential, safety assessment, and functional properties of lactic acid bacteria from camel milk","authors":"Hafsa Ayat El Rahmane Mokhtari ,&nbsp;Omar Hassaine ,&nbsp;Bülent Çeti̇n ,&nbsp;Hacer Meral-Aktaş","doi":"10.1016/j.enzmictec.2025.110676","DOIUrl":"10.1016/j.enzmictec.2025.110676","url":null,"abstract":"<div><div>Camel milk is one of the most valuable food sources in the Algerian desert. Furthermore, it is a strong candidate for use as a functional food because it contains beneficial microorganisms that promote health. The present study investigates 144 lactic acid bacteria isolated from camel milk, examining their probiotic, safety, technological, and antioxidant properties. Of these, 19 lactic acid bacteria showed very high tolerance to the simulated gastric environment and were selected for further analyses. According to the sequence analysis, 15 isolates were identified as <em>Lactiplantibacillus plantarum</em>, 3 as <em>Lactobacillus gasseri</em>, and 1 as <em>Enterococcus faecium</em>. The results indicated that all isolates demonstrated tolerance to bile salts, with levels ranging from 94.86 % to 102.81 %. It was established that none of the strains exhibited undesirable hemolysis, DNase and gelatinase activity, or transmissible antibiotic resistance. Furthermore, the absence of virulence or biogenic amine genes was confirmed. In particular, strain <em>L. gasseri</em> C1 showed remarkably high levels of auto-aggregation and hydrophobicity, which was also revealed in the principal component analysis. Furthermore, the strains exhibited potent antagonistic properties against various foodborne pathogens. Notably, several strains, including <em>L. plantarum</em> A5, A8, and BN2, and <em>L. gasseri</em> C1, showed specific antimicrobial activity against <em>Listeria monocytogenes</em>, potentially due to bacteriocin or other antimicrobial compounds production. Additionally, the majority of the isolates demonstrated bile salt hydrolysis activity, and all strains exhibited antioxidant activity by scavenging DPPH free radicals. Moreover, 11 <em>L. plantarum</em> isolates possessed the <em>gad</em> gene responsible for GABA production. These findings support the potential application of these isolates as probiotics in both food and therapeutic contexts.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110676"},"PeriodicalIF":3.4,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144137985","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Peptone source effects on recombinant protease production and cellular responses in yeast","authors":"Xiufang Liu ,&nbsp;Chufan Xiao ,&nbsp;Xinpeng Yu ,&nbsp;Lin Zheng ,&nbsp;Mouming Zhao ,&nbsp;Mingtao Huang","doi":"10.1016/j.enzmictec.2025.110674","DOIUrl":"10.1016/j.enzmictec.2025.110674","url":null,"abstract":"<div><div>The production of recombinant protease is critical due to their wide range of industrial applications. This study investigates the impact of the peptone switching in the fermentation media on recombinant protease production and cell metabolism. The yeast <em>Saccharomyces cerevisiae</em> was used as the expression host, comparing growth and protease activity in YPD medium (containing bacteriological peptone) and a modified version, YTD medium (containing tryptone). Switching from bacteriological peptone to tryptone resulted in a 35.22% increase in cell density for the protease-producing strain B_lasB2, although protease activity remained undetectable. Peptone switching also resulted in a noticeable shift in broth color from pale yellow to brownish yellow, which was reversed upon deletion of the <em>FET3</em> gene, a homolog of mushroom tyrosinase, and its complex <em>FTR1</em>. Western blot analysis confirmed that the protease was synthesized but remained in an inactive form. RNA sequencing revealed substantial shifts in transcriptional profiles in response to peptone switching. In YTD medium, there was a predominant upregulation of genes involved in protein folding, primarily located in the endoplasmic reticulum lumen. Conversely, in YPD medium, significant downregulation occurred, affecting genes involved in mitochondrial translation and located within the mitochondria. These findings highlight that peptone switching not only affects cell growth and enzyme activity but also induces significant changes in the yeast’s transcriptional landscape. This study provides deeper insights into the metabolic adjustments that yeast undergoes in different fermentation conditions and underscores the complex relationship between peptone source, protease production, and protease activity.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110674"},"PeriodicalIF":3.4,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144137981","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Exploring Helicobacter pylori Histidyl tRNA synthetase as a drug target using biophysical and computational approaches","authors":"Vijayakumar Rajendran,&nbsp;Sekar Kanagaraj","doi":"10.1016/j.enzmictec.2025.110679","DOIUrl":"10.1016/j.enzmictec.2025.110679","url":null,"abstract":"<div><div><em>Helicobacter pylori</em> infections represent a significant global health challenge, particularly due to the increasing prevalence of antibiotic resistance. This study aims to identify novel therapeutic targets by characterising <em>H. pylori</em> Histidyl tRNA synthetase (<em>Hp</em>HRS), an enzyme essential for protein biosynthesis. We successfully cloned, expressed, and purified <em>Hp</em>HRS using affinity chromatography and size exclusion chromatography techniques. Circular dichroism spectroscopy revealed conformational changes in <em>Hp</em>HRS upon substrate binding, with a notable decrease in α-helical content and an increase in β-sheet structures. Fluorescence quenching studies confirmed the binding of L-histidine and ATP to the enzyme's active site. Virtual screening of the ZINC database identified two potential inhibitors, ZINC39960778 and ZINC30878996, which exhibited higher affinities than the natural substrate. Molecular dynamics simulations conducted over 100 ns demonstrated stable protein-ligand interactions, with the HRS-Histidyl Adenylate Monophosphate (HAM) complex showing the highest stability. Free energy landscape analysis indicated greater conformational freedom in ligand-bound complexes than apoproteins. These findings provide valuable insights into the structure and function of <em>Hp</em>HRS, contributing to the development of new antibacterial agents targeting this crucial enzyme in <em>H. pylori</em>. Given the growing concern regarding antibiotic resistance, this study presents a promising avenue for designing new therapeutic strategies against <em>H. pylori</em> infections. Further research should focus on the experimental validation of the identified inhibitors and optimisation to develop potent and selective <em>Hp</em>HRS inhibitors as potential antibacterial candidates.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110679"},"PeriodicalIF":3.4,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144154501","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Peptidases production by Sordariomycetes sp fungus from Manihot esculenta Crantz waste: Application in gluten hydrolysis","authors":"José Carlos Andrade Neto ,&nbsp;Andreia de Araújo Morandim-Giannetti ,&nbsp;Rafael Cerioni Tognato ,&nbsp;Maria Aparecida Juliano ,&nbsp;Adriana Karaoglanovic Carmona ,&nbsp;Patricia Alessandra Bersanetti","doi":"10.1016/j.enzmictec.2025.110678","DOIUrl":"10.1016/j.enzmictec.2025.110678","url":null,"abstract":"<div><div>With the increasing incidence of problems related to gluten intolerance, many studies are being conducted to develop effective treatments and alternatives for gluten digestion. In this context, this study investigated peptidases produced by endophytic fungi isolated from cassava residues capable of hydrolyzing gluten. Twelve fungi were isolated, identified via DNA sequencing, and evaluated for their potential to produce peptidases with this potential. <em>Sordariomycetes</em> sp. (ST15) presented the highest specific peptidase activity to hydrolyze gluten, determined via fluorescence spectroscopy. Therefore, this fungus was selected to perform the optimization step of producing this peptidase. A composite rotational design with a central point (DCCR) was used to evaluate the influence of pH, temperature, and time on fermentation. The ideal conditions for producing the peptidase of interest were pH 5.2, 27 °C, and 11 days. According to the profile obtained via HPLC, the peptidase-enriched extract demonstrated significant gluten hydrolysis potential, efficiently breaking down gliadin and glutenin proteins within two hours of reaction. These findings highlight the potential of ST15 peptidase as a biocatalyst for gluten hydrolysis, offering a promising alternative for controlling gluten intolerance.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110678"},"PeriodicalIF":3.4,"publicationDate":"2025-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144137982","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of functional ricinoleic acid ergosterol ester by Proteus vulgaris K80 lipase-mediated transesterification","authors":"Ka Yeong Lee,&nbsp;Se Hyeon Park,&nbsp;Hyung Kwoun Kim","doi":"10.1016/j.enzmictec.2025.110672","DOIUrl":"10.1016/j.enzmictec.2025.110672","url":null,"abstract":"<div><div>Chemical preservatives have been traditionally used to enhance the shelf life of cosmetics; however, due to rising concerns regarding their potential adverse effects on human health, there has been an increasing shift towards the use of natural antibacterial agents. Castor oil, predominantly composed of ricinoleic acid, has demonstrated potential as an antibacterial agent. This study aimed to synthesize a multifunctional compound by combining ricinoleic acid, known for its antimicrobial properties, with ergosterol, recognized for its cholesterol-lowering effects. In this study, we synthesized ricinoleic acid ergosterol ester (RAEE) using castor oil and ergosterol as substrates and <em>Proteus vulgaris</em> K80 lipase as the catalyst. RAEE was purified using Prep-LC and its purity was verified through LC-MS analysis. Zeta potential measurements on bacterial cell membranes indicated RAEE's capability to adhere to bacterial surfaces. When administered in an emulsion formulation, RAEE exhibited antibacterial activity against <em>Bacillus subtilis</em> and <em>Pseudomonas fluorescens</em>. Additionally, propidium iodide uptake assays and fluorescence microscopy showed that RAEE induced bacterial cell death by increasing membrane permeability. Scanning electron microscopy of RAEE-treated bacteria revealed roughened cell surfaces with abnormal features, illustrating RAEE's substantial potential as a natural preservative in the cosmetics industry.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110672"},"PeriodicalIF":3.4,"publicationDate":"2025-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144106757","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Hyperbranched polymer-crosslinked laccase aggregates for efficient aerobic oxidation of alcohols","authors":"Yan Peng ,&nbsp;Xiaorong Xiong ,&nbsp;Meishuang Qiu,&nbsp;Yizhuo Lu,&nbsp;Tianyou Chen,&nbsp;Zushun Xu","doi":"10.1016/j.enzmictec.2025.110673","DOIUrl":"10.1016/j.enzmictec.2025.110673","url":null,"abstract":"<div><div>The crosslinked enzyme aggregate (CLEA) technique has been developed as an easy and convenient strategy for carrier-free immobilization of enzymes. However, the irregular voids of enzyme aggregates limit the controlled crosslinking process by using regular crosslinkers such as glutaraldehyde. To overcome this limitation, here we have developed a simple strategy for the preparation of hyperbranched polymer-crosslinked laccase aggregates (HPCLEAs). Hyperbranched polymers were generated in voids of laccase aggregates, and the <em>in situ</em> crosslinking through the formation of hyperbranched polymers provided access to the void-adaptive crosslinking process. These HPCLEAs had irregular shapes and sizes of ∼2–10 μm. 99 % of the initial activity was maintained under the optimized preparation conditions. Further incorporation of 2,2,6,6-tetramethyl-1-piperidine-<em>N</em>-oxyl (TEMPO) facilitated the proximity between laccase and TEMPO, resulting in efficient aerobic oxidation of alcohols. Additionally, these catalysts could be easily recovered and reused four times with a slight loss of activity. This strategy may open an avenue for the rational design and co-immobilization of enzyme and molecular catalysts used for chemoenzymatic catalysis.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110673"},"PeriodicalIF":3.4,"publicationDate":"2025-05-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144068173","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Unlocking lignin valorisation: Oxyfunctionalization of lignin dimer model compounds by unspecific peroxygenases","authors":"Essi Rytkönen,&nbsp;Juha Rouvinen,&nbsp;Janne Jänis","doi":"10.1016/j.enzmictec.2025.110661","DOIUrl":"10.1016/j.enzmictec.2025.110661","url":null,"abstract":"<div><div>Lignin is an abundantly available biopolymer composed of three structural units, linked by a complex network of bonds, including a high proportion of β-O-4 ether linkages. As a renewable carbon source, it can be depolymerised into a variety of small aromatic compounds such as monophenols. Enzymatic bioprocessing offers a promising alternative to traditional chemical lignin degradation strategies, potentially producing value-added compounds, such as monoaromatics. Unspecific peroxygenases (UPOs) are promising enzymes for lignin bioprocessing due to their ability to catalyse aromatic oxidation and demethylation reactions, which are critical for lignin valorisation. In this study, thirteen different UPOs were evaluated for their oxidation potential with two lignin dimer model compounds, guaiacylglycerol-β-guaiacyl ether and veratrylglycerol-β-guaiacyl ether. Both compounds were successfully processed, yielding a wide range of products, e.g., via C_α-oxidation, demethylation, and bond cleavage reactions. Notably, the cleavages frequently occurred at the C_β–O ether bond, a major linkage between the lignin monomers, being beneficial for lignin degradation and subsequent valorisation. Some of the identified products, such as vanillin, are of interest either as valuable end-products or as precursors for further conversion into specialty chemicals.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"189 ","pages":"Article 110661"},"PeriodicalIF":3.4,"publicationDate":"2025-05-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144084496","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}