Enzyme and Microbial Technology最新文献

{"title":"Improving isobutanol and 2-ketoisovalerate production by reducing by-product synthesis in Klebsiella pneumoniae","authors":"Wenqi Wang ,&nbsp;Shaoqi Sun ,&nbsp;Weiyan Jiang ,&nbsp;Xinjie Bian ,&nbsp;Taiyu Liu ,&nbsp;Frank Baganz ,&nbsp;Dexin Wang ,&nbsp;Jian Hao","doi":"10.1016/j.enzmictec.2026.110838","DOIUrl":"10.1016/j.enzmictec.2026.110838","url":null,"abstract":"<div><div>Isobutanol is a promising next-generation biofuel with a high energy density and is considered a sustainable aviation fuel precursor. <em>Klebsiella pneumoniae</em> is an industrial workhorse microorganism used for the production of various chemicals. An endogenous isobutanol synthesis pathway, interconnected with the branched-chain amino acid and 2,3-butanediol biosynthesis pathways, has been identified in <em>K. pneumoniae</em>. However, isobutanol production by <em>K. pneumoniae</em> is inefficient due to the substantial formation of by-products. In this study, we enhanced isobutanol synthesis by systematically engineering <em>K. pneumoniae</em> to reduce by-product accumulation. The synthesis of 2-hydroxyisovalerate was reduced by knocking out <em>panE</em>. Formate synthesis was eliminated by disrupting <em>pflB</em>. The production of ethanol, acetate, and succinate was reduced by deleting <em>aceE</em>. Pyruvate accumulation was alleviated by overexpressing <em>budB</em>. In batch fermentation, the engineered strain produced 13.97 g/L of 2-ketoisovalerate, a key intermediate in the isobutanol pathway, with a conversion ratio of 0.43 mol/mol glucose. Fed-batch fermentation further increased the 2-ketoisovalerate titer to 26.63 g/L after 54 h of cultivation. The decarboxylation of 2-ketoisovalerate to isobutyraldehyde is catalysed by IpdC. Overexpression of the <em>ipdC</em> T290L variant shifted the major product from 2-ketoisovalerate to isobutanol, resulting in a batch fermentation titer of 5.32 g/L isobutanol and a conversion ratio of 0.28 mol/mol glucose. Fed-batch fermentation further increased the final isobutanol titer to 10.32 g/L after 52 h of cultivation. This study establishes an efficient strategy for high-level production of isobutanol or 2-ketoisovalerate in <em>K. pneumoniae</em>.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"197 ","pages":"Article 110838"},"PeriodicalIF":3.7,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147347268","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":"Beyond depolymerization rates: Health‑aligned benchmarking for PET‑degrading enzymes in enzyme and microbial technology","authors":"M. Vijayasimha ,&nbsp;M. Srikanth ,&nbsp;Labishetty Sai Charan","doi":"10.1016/j.enzmictec.2026.110839","DOIUrl":"10.1016/j.enzmictec.2026.110839","url":null,"abstract":"<div><div>Polyethylene terephthalate (PET) hydrolases are commonly benchmarked according to depolymerization efficiency, monomer yield, and reaction kinetics. Recent advances—including anchor-peptide fusion strategies and computationally engineered enzymes—have substantially improved catalytic performance under laboratory and industrially relevant conditions. However, performance-focused benchmarking alone does not capture how enzymatic degradation may influence particle fate, transient fragment formation, or downstream process compatibility. Here, we propose an exposure-aligned benchmarking framework that complements conventional depolymerization metrics by integrating physicochemical indicators linked to potential human and environmental exposure pathways. The framework is structured around three tiers representing inhalation-relevant PET microfibres, ingestion-relevant packaging fragments, and industrial post-consumer PET feedstocks. For each tier, we outline harmonized reporting parameters including crystallinity, surface aging, particle-size distribution trajectories, and downstream compatibility with filtration and monomer-purification steps. Importantly, the framework does not assume adverse health outcomes from enzymatic recycling products. Instead, it provides standardized descriptors that enable comparison of particle behavior across enzyme systems, substrates, and reaction conditions. We further clarify the mechanistic role of polymer crystallinity in defining residual fragments and highlight experimental gaps requiring matched-yield comparisons between engineered and wild-type enzymes. By aligning enzyme benchmarking with exposure-relevant physicochemical metrics—without imposing routine toxicological testing—this approach supports reproducibility, industrial relevance, and responsible innovation in PET biocatalysis. Adoption of such complementary benchmarks may facilitate the transition from rate-driven optimization toward decision-grade evaluation of next-generation PET-degrading enzymes.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"197 ","pages":"Article 110839"},"PeriodicalIF":3.7,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147372174","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":"Comparative evaluation of l-theanine synthetases coupled with PPK2 based ATP regeneration under buffer-free and Mn2 + optimized conditions","authors":"Kyungjae Yu ,&nbsp;Hyun Gi Koh ,&nbsp;Byung Wook Lee ,&nbsp;Haeng-Geun Cha ,&nbsp;Gaeul Kim ,&nbsp;Yoon Jung Jung ,&nbsp;Jung Bin Shin ,&nbsp;Jung-Oh Ahn ,&nbsp;Yung-Hun Yang ,&nbsp;Hee Taek Kim ,&nbsp;Hyung-Wook Jang ,&nbsp;Minjeong Sohn ,&nbsp;See-Hyoung Park ,&nbsp;Kyungmoon Park","doi":"10.1016/j.enzmictec.2026.110834","DOIUrl":"10.1016/j.enzmictec.2026.110834","url":null,"abstract":"<div><div><span>l</span>-theanine (γ-glutamylethylamide) is a bioactive amino acid widely valued for its functional and nutraceutical applications. While enzymatic synthesis using γ-glutamylmethylamide synthetase (GMAS) has been extensively studied, the potential of γ-glutamylcysteine synthetase (GCS) as an alternative biocatalyst remains underexplored. In this study, a high-substrate, buffer-free whole-cell conversion system was established for <span>l</span>-theanine production using <em>Escherichia coli</em> expressing either GMAS from <em>Methylovorus mays</em> (MmGMAS) or the GCS from <em>E. coli</em> (ecGCS), with an integrated ATP regeneration mechanism driven by polyphosphate kinase 2 (PPK2). <em>In silico</em> predictions using CatPred, a machine learning-based catalyst prediction tool, indicated that ecGCS exhibits catalytic efficiency comparable to or exceeding that of MmGMAS, which was consistent with the experimental results. Among six PPK2 variants tested, the enzyme from <em>Rhodobacter sphaeroides</em> (PPK2–6) was identified as the most suitable ATP regeneration module, enabling approximately 90% reduction in ATP input while maintaining high <span>l</span>-theanine yields. Both MmGMAS-PPK2–6 and ecGCS-PPK2–6 systems produced 47.9 g/L (34.4%) and 44.5 g/L (31.9%) of <span>l</span>-theanine, respectively, starting from 800 mM substrates. Furthermore, it was confirmed that <span>l</span>-theanine production was not compromised in the absence of exogenous buffers, which may also facilitate downstream processing. This work represents the first demonstration of efficient <span>l</span>-theanine production using native ecGCS under process-relevant conditions, and highlights its potential as a complementary or alternative platform to GMAS-based biosynthesis.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"197 ","pages":"Article 110834"},"PeriodicalIF":3.7,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147321544","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":"Tailored high-cell-density fed-batch cultivation and induction strategies for optimized production of a low-immunogenic L-asparaginase mutant in Escherichia coli","authors":"Larissa Pereira Brumano ,&nbsp;Diego Grumbach ,&nbsp;Flaviana da Silva Chaves ,&nbsp;Gisele Monteiro ,&nbsp;Adalberto Pessoa Jr ,&nbsp;Solange I. Mussatto","doi":"10.1016/j.enzmictec.2026.110836","DOIUrl":"10.1016/j.enzmictec.2026.110836","url":null,"abstract":"<div><div>An integrated upstream process was developed for the high-level production of a low-immunogenic <span>L</span>-asparaginase mutant (EcaII P40S/S206C) in <em>Escherichia coli</em>, combining high-cell-density fed-batch cultivation with controlled induction and post-induction nutrient feeding. Biomass accumulation was achieved by exponential substrate feeding, followed by pH-stat-based nutrient supply during the expression phase. Induction protocols were optimized using biomass-specific IPTG dosing (µmol IPTG/g_cell), applied either as a pulse or via exponential feeding. This combined strategy resulted in a maximum volumetric enzyme activity of 134,516 U/L and a specific productivity of 3387 U/g_cell, corresponding to 91-fold and 24-fold increases, respectively, compared with standard batch cultivation. Overall, these results indicate that the coordinated control of feeding strategy and induction conditions substantially improves both volumetric and cell-specific productivity of recombinant <span>L</span>-asparaginase and provides a robust upstream framework for the efficient manufacture of improved enzyme variants.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"197 ","pages":"Article 110836"},"PeriodicalIF":3.7,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147354441","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":"Urolithin 9-dehydroxylase from Enterocloster bolteae JCM 12243T catalyzing regiospecific dehydroxylation of urolithins","authors":"Anno Katasho ,&nbsp;Kanako Kumazawa ,&nbsp;Hiroko Watanabe ,&nbsp;Takanori Nakajima ,&nbsp;Natsuno Chiba ,&nbsp;Hiroaki Yamamoto ,&nbsp;Shigenobu Kishino ,&nbsp;Jun Ogawa","doi":"10.1016/j.enzmictec.2026.110837","DOIUrl":"10.1016/j.enzmictec.2026.110837","url":null,"abstract":"<div><div>Urolithins are metabolites derived from ellagic acid, a compound that is present in many plants, including pomegranate, via the action of gut microorganisms. Among them, urolithin A exhibits antioxidant and anti-inflammatory activity and promotes autophagy, making it a potential contributor to human health. <em>Enterocloster bolteae</em> JCM 12243^T, isolated from human feces, is able to convert urolithin C into urolithin A. In previous studies, the urolithin C dehydroxylase encoded by the <em>ucdCFO</em> (or <em>ucdhABC</em>) from <em>E. bolteae</em> DSM 15670^T (=JCM 12243^T) was identified through proteomic or transcriptomic analyses. In contrast, we aimed to identify the enzymes responsible for the reaction using through purification from cell extracts of the wild type active strain. Our results show that UcdCFO/UcdhABC is the sole catalyst of urolithin C dehydroxylation to urolithin A in this bacterium. To further characterize the enzyme, we obtained it from the <em>Rhodococcus erythropolis</em> L88 transformant expressing the codon-optimized genes and analyzed its properties. The purified enzyme catalyzed dehydroxylation at the 9-position of five urolithins, indicating that the enzyme is a urolithin 9-dehydroxylase. Kinetic analysis indicated that the enzyme has a high catalytic activity toward urolithin M6 with almost the same activities to urolithin M5 and urolithin C. This enzyme exhibited maximum activity for the conversion of urolithin C into urolithin A between pH 6.5 and 7.5 and at 37 °C. This findings provide valuable information for the efficient fermentation-based production of urolithin A, which exerts health-promoting effects.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"197 ","pages":"Article 110837"},"PeriodicalIF":3.7,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147376563","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":"Impacts of microchannel parameters on CLEAs immobilization","authors":"Chang Liu,&nbsp;Zihao Yin,&nbsp;Chenfeng Ma,&nbsp;Shuguang Wang","doi":"10.1016/j.enzmictec.2026.110835","DOIUrl":"10.1016/j.enzmictec.2026.110835","url":null,"abstract":"<div><div>Cross-linked enzyme aggregates (CLEAs) are suitable to use in microchemical technology, but CLEAs shortcomings limit their application. The combination of CLEAs and microchannel can overcome CLEAs shortcomings. However, it is unclear how CLEAs immobilization is affected by microchannel parameters. The effects of microchannel (geometry, diameter, length) and its groove (shape, depth, size, density) on urease-CLEAs immobilization were investigated. Moreover, CFD simulation was conducted to reveal the effects of CLEAs particle size on fluid dynamic in microchannel. Results showed that microchannel reactor with immobilized urease-CLEAs (MRIC) had the highest activity under the following optimal conditions: Wave-type microchannel, 50.0 cm in microchannel length, 2.0 mm in microchannel diameter, and triangular groove that was 1.0 mm in depth, 1.2 mm² in size, and 2.0 individuals/cm² in density. MRIC activity was up to 1.450 U/cm², which was 4.63 times higher than that of the microchannel reactor with free urease (MRFU). Moreover, MRIC showed better reusability than MRFU. CFD simulation confirmed that the presence of CLEAs disturbed local flow velocity in microchannel. This study indicates that the combination of CLEAs and microchannel is a promising strategy to prepare enzymatic microchannel reactor.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"197 ","pages":"Article 110835"},"PeriodicalIF":3.7,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147303425","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":"Enzymatic hydrolysis of milk thistle protein: Influence of protease types on structure and biological activity","authors":"Ying Zhang ,&nbsp;Zihui Qiao ,&nbsp;Yuxin Zhang ,&nbsp;Rihan Zhao ,&nbsp;Xiaoqiang Chen","doi":"10.1016/j.enzmictec.2026.110848","DOIUrl":"10.1016/j.enzmictec.2026.110848","url":null,"abstract":"<div><div>In this study, milk thistle protein (MTP) was hydrolyzed by neutral protease, alkaline protease and papain to obtain neutral protease hydrolysate (NPH), alkaline protease hydrolysate (APH) and papain enzymatic hydrolysate (PEH), respectively. The influence of enzymes on the structure, the antioxidant activity and the α-glucosidase inhibitory activity of MTP were evaluated. The results showed that the essential amino acid contents of NPH, APH, PEH and MTP were 29.54%, 29.76%, 27.44% and 29.05%, NPH exhibited the highest antioxidant activity (DPPH IC₅₀ = 0.37 ± 0.04 mg/mL, ABTS IC₅₀ = 0.32 ± 0.01 mg/mL) and α-glucosidase inhibitory activity (IC₅₀ = 10.21 ± 0.48 mg/mL). In addition, the molecular weight and thermal stability of the enzyme-decomposed MTP decreased, that the hydrogen bonds and hydrophobic regions were destroyed and that the antioxidant activity and α-glucosidase inhibitory activity increased. It can be seen from this that both neutral protease and alkaline protease can improve the nutritional value of proteins. The glucosidase inhibitory activity of NPH may also have potential applications in blood glucose reduction.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"197 ","pages":"Article 110848"},"PeriodicalIF":3.7,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147372219","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":"Biochemical characterization of heterologously expressed Thiomonas delicata arsenite oxidase subunits (AioA and AioB)","authors":"Mahesh Mannacharaju,&nbsp;Soichiro Tanaka,&nbsp;Naoko Okibe","doi":"10.1016/j.enzmictec.2026.110833","DOIUrl":"10.1016/j.enzmictec.2026.110833","url":null,"abstract":"<div><div>Arsenite oxidase (Aio) plays a central role in the microbial oxidation of As(III) to the generally less toxic and more easily removable As(V). In this study, the <em>aioA</em> and <em>aioB</em> genes from <em>Thiomonas delicata</em> strain DSM 16361 were heterologously expressed in <em>Escherichia coli</em> BL21 (DE3) using the pRSFDuet–1 system, and the recombinant proteins were purified under optimized conditions. The two subunits were purified individually, and their activities were evaluated alone and after reconstitution. AioA displayed markedly higher enzyme activity than AioB, consistent with its role as the catalytic center, whereas purified AioB alone showed no detectable As(III) oxidation activity, supporting its function in intramolecular electron transfer between subunits. When AioA and AioB were combined in a 1:1 molar ratio, the catalytic efficiency (kcat/Km: 1246 ± 26 M⁻¹/s) and Vmax (38 ± 2 µmol/min/mg) increased compared to AioA alone, confirming that AioB enhances electron flux and overall oxidation performance. The purified enzyme exhibited maximum activity at pH 7.0 and 40 °C and retained activity across a broad pH (4–8) and temperature (20–50 °C) range. Activity was largely unaffected by most metal ions and anions tested, although Triton X–100 significantly inhibited catalysis. Batch oxidation tests using purified AioA demonstrated rapid conversion of As(III) under environmentally relevant concentrations: 20 mg/L was fully oxidized within 15 min, and 40 mg/L within 60 min, while higher loadings showed partial conversion within the same reaction time. These findings highlight the potential application of recombinant AioA in enzymatic arsenic remediation and provide a foundation for designing AioA–based biocatalytic treatment systems for contaminated waters.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"197 ","pages":"Article 110833"},"PeriodicalIF":3.7,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147303405","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":"Retraction notice to “Identification and recombinant expression of a novel defluorinase from Rhodococcus jostii RHA1, for defluorination and biotransformation of the PFAS compound 6:2 fluorotelomer carboxylic acid” [Enzyme Microb. Technol. 191 (2025) 110724]","authors":"Eustace Y. Fernando","doi":"10.1016/j.enzmictec.2026.110823","DOIUrl":"10.1016/j.enzmictec.2026.110823","url":null,"abstract":"","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"196 ","pages":"Article 110823"},"PeriodicalIF":3.7,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146156558","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":"Dual antioxidant and antibacterial potential of β-cryptoxanthin and a novel biosurfactant from Kocuria marina DAGII","authors":"Daiji Brahma ,&nbsp;Anwesha Mahanty ,&nbsp;Prity Chatterjee ,&nbsp;Riya Dey ,&nbsp;Abheerup Sarker ,&nbsp;Sagnik Kulavi ,&nbsp;Debjani Dutta","doi":"10.1016/j.enzmictec.2026.110821","DOIUrl":"10.1016/j.enzmictec.2026.110821","url":null,"abstract":"<div><div>In the present study, the combinatory role of beta-cryptoxanthin (β-CRX) and novel biosurfactant (BS) produced by <em>Kocuria marina</em> DAGII was explored. Spectral analysis of biosurfactant showed <em>a</em> strong peak at 265 nm. Characterization of biosurfactant was performed using CHNSO (carbon, hydrogen, nitrogen, sulphur, and oxygen) and MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis. MALDI-TOF spectra showed an intense peak at 379.7 <em>m/z</em>, indicating the presence of structural components like sugars, lipids, and clusters of fragment ions closely related to rhamnolipid (glycolipid) like biosurfactant. CHNSO analysis of partially purified biosurfactant revealed the presence of nitrogen (4.675 %), carbon (30.815 %), hydrogen (7.417 %), and oxygen (25.428 %). A combination of BS and β-CRX demonstrated higher antioxidant activity compared to BS alone. The highest inhibition against <em>Staphylococcus epidermidis</em> MTCC 3615 and <em>Pseudomonas aeruginosa</em> MTCC 741 was observed for the combined effect of BS (32 mg/ml) and β-CRX (0.1 mg/ml). However, the lowest antibacterial activity was observed against <em>Staphylococcus aureus</em> MTCC 96 (0.3 ± 0.041 cm), likely due to its strong biofilm formation. Membrane integrity and permeability assays revealed enhanced activity against Gram-positive <em>Staphylococcus epidermidis</em> having OD₂₆₀ value 1.23 ± 0.060 and OD₄₂₀value 0.157 ± 0.01. The increased outer membrane permeability was assessed through the NPN uptake assay in <em>Pseudomonas aeruginosa</em>. Antibiofilm assay showed good antibiofilm activity (66.14 ± 0.13 %) against <em>Staphylococcus epidermidis</em> for combined effect of BS (32 mg/ml) and β-CRX (0.1 mg/ml). Overall, the study suggests that a combination of BS and β-CRX has promising potential as a dual antioxidant and antibacterial agent, particularly effective against these tested opportunistic skin pathogens.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"196 ","pages":"Article 110821"},"PeriodicalIF":3.7,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146071142","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}