Enzyme and Microbial Technology最新文献

{"title":"Breaking the CREB–CBP alliance: Progress, challenges, and therapeutic promise of small-molecule and peptide disruptors of the pKID–KIX interaction","authors":"Hassan A. Rudayni","doi":"10.1016/j.enzmictec.2025.110734","DOIUrl":"10.1016/j.enzmictec.2025.110734","url":null,"abstract":"<div><div>The kinase-inducible domain (pKID) of the transcription factor CREB engages the KIX domain of the co-activator CBP/p300 to drive signal-dependent gene expression that underpins cell proliferation, metabolism and survival. Aberrant CREB–CBP signaling is now implicated in numerous cancers and metabolic disorders, yet until recently the shallow, dynamic pKID–KIX interface was viewed as chemically intractable. This review integrates two decades of progress that overturns that paradigm. We first dissect the structural and allosteric features of KIX that enable coupled folding-and-binding of pKID and reveal hidden ligandable pockets. We then survey the expanding inhibitor repertoire—from early micromolar naphthols (KG-501) through nanomolar naphthamides (666−15) and orally tractable pro-drugs, to high-affinity stapled and D-peptide mimetics—highlighting the assays, structure–activity relationships and pharmacokinetic optimization that have driven each advance. Biophysical and computational insights, including ¹⁹F NMR ligandability maps and millisecond-scale molecular-dynamics trajectories, are shown to guide next-generation design and machine-learning pipelines. Pre-clinical data demonstrate that disrupting CREB–CBP selectively suppresses tumor growth with favorable tolerability, and we outline opportunities for combination therapies, degrader strategies and indication expansion into metabolic and neurocognitive disease. Collectively, these findings position the CREB–CBP interaction as a tractable, multi-modal drug target poised for first-in-human exploration.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110734"},"PeriodicalIF":3.7,"publicationDate":"2025-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144841939","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":"Isolation, expression and characterization of a novel thermo-acid/alkali-stable GH10 xylanase BsXynA from Bacillus safensis L7 and its potential for xylooligosaccharide production and animal feed saccharification","authors":"Ting Zhang,&nbsp;Zhong Cheng,&nbsp;YuMei Fan,&nbsp;YuXin Lan,&nbsp;HuiLan Shu,&nbsp;JinHua Chen,&nbsp;FengCheng Jin,&nbsp;LiYuan Qin,&nbsp;DongPing Feng","doi":"10.1016/j.enzmictec.2025.110735","DOIUrl":"10.1016/j.enzmictec.2025.110735","url":null,"abstract":"<div><div>Xylanases have wide applications in agro-industrial processes. This study reports the discovery and characterization of a novel thermo-acid/alkali-stable GH10 xylanase (BsXynA) from <em>Bacillus safensis</em> L7. The xylanase gene (<em>BsxynA</em>) was cloned and expressed in <em>Escherichia coli</em> BL21 (DE3), yielding a protein of approximately 64 kDa. BsXynA exhibited optimal activity (17.33 U/mg) on beechwood xylan at pH 6.0 and 60°C. Moreover, BsXynA exhibited remarkable thermo-acid/alkali stability, retaining over 60 % activity at pH 5.0–8.0 after 60 min at 60°C and over 80 % activity after 14 days at 4°C within pH 6.0–9.0. Additionally, the enzyme tolerated 50°C and various chemicals, with a half-life of over 16 days. It was activated by K⁺, Na⁺, Ca²⁺, Ba²⁺, and Mg²⁺ ions but inhibited by Zn²⁺, Cu²⁺, and SDS. BsXynA hydrolyzed various xylans but not glucose-based polysaccharides. <em>K</em>_m, <em>V</em>_max, <em>k</em>_cat, and <em>k</em>_cat/<em>K</em>_m for beechwood xylan hydrolysis were found to be 6.61 mg/mL, 24.24 µmol·min⁻¹·mg⁻¹, 15.71 s⁻¹, and 2.38 mL·s⁻¹·mg⁻¹ respectively. Thin-layer chromatography (TLC) analysis showed that BsXynA is an endo-type xylanase, which hydrolyzes beechwood xylan to produce mainly xylobiose (X2) and xylotetraose (X4), with no xylose detected. Furthermore, BsXynA improved animal feed saccharification, making it a promising biocatalyst for biotechnological applications.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110735"},"PeriodicalIF":3.7,"publicationDate":"2025-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144841943","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":"Ethyl lactate synthesis in organic media using a magnetic supported CALB","authors":"Paula Nicolás ,&nbsp;Verónica L. Lassalle ,&nbsp;María Luján Ferreira","doi":"10.1016/j.enzmictec.2025.110732","DOIUrl":"10.1016/j.enzmictec.2025.110732","url":null,"abstract":"<div><div>The growing demand for sustainable chemical processes has spurred interest in enzymatic synthesis, particularly for valuable compounds like ethyl lactate. Traditional chemical methods often suffer from drawbacks, highlighting the potential of enzymatic catalysis using immobilized lipases. This study evaluated the performance of magnetic biocatalyst, prepared by immobilizing <em>Candida antarctica</em> lipase B (CALB) on magnetic nanoparticles, for the batch synthesis of ethyl lactate in hexane. Initial experiments using free CALB and commercial Novozym435 proved problematic due to enzyme denaturation and support instability, respectively. While titration-based methods for monitoring the reaction were found to be unreliable due to lactic acid's complex behavior in the reaction medium, titratable acidity reduction suggested an optimal lactic acid to ethanol molar ratio of 1/10. Subsequent HPLC analysis revealed that the magnetic biocatalyst maintained a consistent conversion (%) at higher lactic acid concentrations (up to 17 mg/mL at 45°C, with conversion above 60 % in 5 h), demonstrating its potential for processing larger amounts of substrate. The initial reaction rate was estimated to be 3.8 mM/h. The study also identified experimental challenges in accurate lactic acid quantification and potential catalyst degradation. In conclusion, the magnetic CALB biocatalyst shows promising activity and stability for ethyl lactate synthesis, especially at higher substrate loads, paving the way for further optimization and application in sustainable production.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110732"},"PeriodicalIF":3.7,"publicationDate":"2025-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144828379","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":"Elucidation of biochemical attributes and enzymatic activity of agarase from Saccharophagus degradans 2–40","authors":"Anoth Maharjan ,&nbsp;Beom Soo Kim","doi":"10.1016/j.enzmictec.2025.110733","DOIUrl":"10.1016/j.enzmictec.2025.110733","url":null,"abstract":"<div><div><em>Saccharophagus degradans</em> 2–40 exhibits agarolytic activity, effectively degrading agar into galactose. Both endo- and exo-agarase, as well as neoagarobiose hydrolase (NABH), play important roles in agar saccharification for the production of monosugars. This study characterizes a novel agarase enzyme from <em>S. degradans</em> 2–40, a marine bacterium renowned for its exceptional polysaccharide-degrading capabilities. We hypothesized that this strain would harbor an efficient and robust agarase with desirable properties for saccharification processes. Following isolation and purification, the agarase underwent biochemical analysis, revealing optimal activity at moderate temperatures and a broad pH range. Furthermore, the fusion of Aga50D with NABH enhanced the catalytic efficiency from 1.873 ± 0.22 (mg/mL)⁻¹s⁻¹ to 4.826 ± 0.19 (mg/mL)⁻¹s⁻¹. In contrast to chemical hydrolysis, enzymatic treatment using agarase offers a more selective, eco-friendly, and high-yield alternative, minimizing by-product formation and preserving functional sugar moieties. The enzyme's ability to produce neoagarobiose (NA2) as its primary product, without any intermediates, makes it an attractive biocatalyst for the production of bioactive oligosaccharides. This study highlights the potential of <em>S. degradans</em> 2–40 as a valuable source of enzymes for industrial biotechnology applications, particularly in the sustainable conversion of marine biomass into high-value products.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110733"},"PeriodicalIF":3.7,"publicationDate":"2025-08-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144826545","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":"NADPH regeneration for efficient biosynthesis of indigo by flavin-containing monooxygenase and formate dehydrogenase","authors":"Yingying Zhu ,&nbsp;Dawei Ni ,&nbsp;Zeyu Li ,&nbsp;Zhebin Hao ,&nbsp;Liang Wang ,&nbsp;Wanmeng Mu","doi":"10.1016/j.enzmictec.2025.110731","DOIUrl":"10.1016/j.enzmictec.2025.110731","url":null,"abstract":"<div><div>Indigo is an important blue pigment widely used in textile, food, and medicine industries. Biological production of indigo attracts increasing attention recently. Cell factory production of indigo encounters the problem of the toxicity of the precursor indole. Enzymatic production is the alternative biological approach, however, NADPH regeneration should be solved. In this study, flavin-containing monooxygenase from <em>Methylophaga aminisulfidivorans</em> was used for enzymatic production of indigo from indole and formate dehydrogenase from <em>Pseudomonas</em> sp. 101 was co-expressed for NADPH regeneration. Indigo production was enhanced by combination of molecular modification, promoter engineering, and translation initiation region engineering. Finally, 0.183 g/L of indigo was produced from 0.5 g/L of indole and 0.5 mM of sodium formate, with the conversion ratio of 32.5 %. This study demonstrates a feasible and effective strategy for enzymatic production of indigo.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110731"},"PeriodicalIF":3.7,"publicationDate":"2025-08-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144780037","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":"Preparation of ginsenoside Rd using a novel α-L-arabinofuranosidase BpAbf51A from Bacillus pumilus","authors":"Yuzhu Shen ,&nbsp;Yue Yang ,&nbsp;Yudi Song ,&nbsp;Yakun Shan ,&nbsp;Jiaxin Liu ,&nbsp;Yanbo Hu","doi":"10.1016/j.enzmictec.2025.110729","DOIUrl":"10.1016/j.enzmictec.2025.110729","url":null,"abstract":"<div><div>α-L-Arabinofuranosidase has been widely used in the fields of enhancing pasta production quality, fruit juice clarification, enhancing wine flavor, increasing feed utilization rate, and developing special drug ingredients, playing a pivotal role in the food processing, feed, and medical care industries. In this study, a novel α-L-arabinofuranosidase (BpAbf51A), belonging to glycoside hydrolase family 51 (GH51), was cloned from the <em>Bacillus pumilus</em> strain 145 and expressed in <em>Escherichia coli</em> BL21 (DE3), with a molecular weight of approximately 56.0 kDa. BpAbf51A comprises two characteristic domains of the GH51 family: an N-terminal (β/α)₈-barrel catalytic domain and a C-terminal jelly-roll domain. The enzyme exhibits high substrate specificity for <em>p</em>-nitrophenyl-α-L-arabinofuranoside and demonstrates optimal catalytic activity at 50°C and pH 8.0, suggesting its potential for industrial applications under moderate conditions. Notably, BpAbf51A specifically hydrolyzes the arabinofuranosyl moiety at the C-20 position of ginsenoside Rc to produce ginsenoside Rd. Molecular docking and two-dimensional interaction diagrams further revealed that the key amino acid residues, Ser213 and Asn214 of BpAbf51A, form strong hydrogen bonds with ginsenoside Rc. In this study, a novel α-L-arabinofuranosidase, BpAbf51A, has demonstrated significant potential for industrial applications in the production of rare saponins and other glycoside-based natural products, providing new research directions for the development of efficient biocatalysts.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110729"},"PeriodicalIF":3.7,"publicationDate":"2025-08-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144770768","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":"DNA box-assisted T7 transcription techniques combined with Cas13a for detection of the influenza A (H1N1) virus","authors":"Mengyuan Zhou ,&nbsp;He Sun ,&nbsp;Shengjun Bu ,&nbsp;Yao Xu ,&nbsp;Hongyu Zhou ,&nbsp;Ziqin Song ,&nbsp;Zebin Zhang ,&nbsp;Zhuo Hao ,&nbsp;Songling Yu ,&nbsp;Jiayu Wan ,&nbsp;Feng Tang","doi":"10.1016/j.enzmictec.2025.110728","DOIUrl":"10.1016/j.enzmictec.2025.110728","url":null,"abstract":"<div><div>The influenza A (H1N1) virus continues to undergo mutations, posing a serious threat to public health. In this study, an innovative system was developed using a transcriptional isothermal amplification scheme combined with a DNA box for detection of H1N1 RNA. The split T7 promoter was assembled on four edges of the hexahedral DNA box to form two target-capturing robotic arms. Transcribed ssRNA was accurately recognized by the Cas13a system and used the trans-cleavage activity to release a fluorescent signal. As compared to the traditional split T7 technique, the novel DNA box greatly improved the reaction rate and biological stability in complex organisms. The sensor platform strategy enabled stable and accurate detection of H1N1 RNA with detection limits as low as the fM level. In general, the proposed system provided a good sensing tool for virus diagnosis and monitoring with great potential in environmental and public health applications.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110728"},"PeriodicalIF":3.7,"publicationDate":"2025-08-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144756737","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":"Cell surface display of CAL-B in Escherichia coli using the split GFP system","authors":"Jisoo Lee,&nbsp;Jong-In Won","doi":"10.1016/j.enzmictec.2025.110726","DOIUrl":"10.1016/j.enzmictec.2025.110726","url":null,"abstract":"<div><div>Bacterial surface display systems enable the immobilization of proteins on the outer membrane for applications such as peptide library screening, biosensing, and bioadsorption. However, the display efficiency of large proteins remains limited, primarily due to challenges in translocating bulky polypeptides across the membrane. To address this, a split Green Fluorescent Protein (split GFP)-based strategy was evaluated. This method employs two non-fluorescent GFP fragments—GFP11 and GFP1–10—that reassemble into a fluorescent complex when co-localized. In this study, the small GFP fragment (GFP11) was genetically fused to Lipoprotein-Outer Membrane Protein A (Lpp-OmpA) to promote membrane anchoring, while the large GFP fragment (GFP1–10) was fused to <em>Candida antarctica</em> lipase B (CAL-B). The CAL-B-GFP1–10 fusion protein was expressed separately and then incubated with cells displaying Lpp-OmpA-GFP11, facilitating potential reassembly on the cell surface. Restoration of fluorescence served as an indirect indicator of successful surface localization. Enzymatic assays were also performed to compare the activity of CAL-B displayed via the split GFP system versus conventional direct fusion to Lpp-OmpA. The results demonstrated that the split GFP approach can enhance surface display and preserve enzymatic function, offering a promising alternative for displaying large or structurally complex proteins. While further optimization is needed, these findings support the potential of split GFP-assisted strategies in expanding the scope of bacterial surface display applications.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110726"},"PeriodicalIF":3.7,"publicationDate":"2025-07-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144750830","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":"Application of natively expressed chitinase as a sustainable fungal bioshield","authors":"Farah Deeba ,&nbsp;Tarek E. Mazeed ,&nbsp;Davita L. Watkins ,&nbsp;Chad A. Rappleye ,&nbsp;David W. Wood","doi":"10.1016/j.enzmictec.2025.110727","DOIUrl":"10.1016/j.enzmictec.2025.110727","url":null,"abstract":"<div><div>Postharvest losses of fruits and vegetables due to fungal spoilage pose a significant challenge, compounded by growing consumer concerns about the harmful effects of chemical fungicides and the limited effectiveness of traditional food coatings (such as wax and biopolymer formulations) in controlling microorganisms, particularly fungi. In this study, we developed a formulation-free method using a non-modified chitinase from a thermostable strain of <em>Bacillus cereus</em> isolated from soil. The purified chitinase inhibited in vitro mycelium growth of four food-pathogenic fungi: <em>Penicillium digitatum</em>, <em>Neurospora crassa</em>, <em>Aspergillus fumigatus</em>, and <em>Alternaria alternata</em>. Furthermore, when applied directly on strawberry and onion tissue, the purified chitinase inhibited <em>Aspergillus fumigatus</em> and <em>A. niger</em> colonization of the produce. This demonstrates the addition of chitinase provides a cost-effective and non-toxic alternative as a bio-active food coating material to prevent fungal fruit and vegetable spoilage and extend food shelf life.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110727"},"PeriodicalIF":3.7,"publicationDate":"2025-07-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144766999","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":"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","authors":"Eustace Y. Fernando","doi":"10.1016/j.enzmictec.2025.110724","DOIUrl":"10.1016/j.enzmictec.2025.110724","url":null,"abstract":"<div><div>Poly and per fluorinated substances (PFAS) are emerging contaminants of concern that are thought to be involved in causing numerous adverse health effects, such as immunosuppression, increased chance of cancer development, and altered levels of hepatic enzyme levels in humans. However, PFAS are considered highly persistent and resistant to biodegradation given the fact that the C-F bond can have a bond dissociation energy of up to 544 kJ/mol. Though many studies have reported PFAS biodefluorination by bacterial isolates and microbial communities, little is known regarding the molecular foundations for biodefluorination. In this study, a novel defluorinase was identified, that is responsible for the biodefluorination of 6:2 fluorotelomer carboxylic acid (6:2 FTCA) in <em>R</em>.<em>jostii</em> RHA1 using the combination of transposome-based insertional mutagenesis and heterologous expression. From a library of 417 <em>R</em>.<em>jostii</em> RHA1. mutants, 3 individual mutants lost their ability for defluorination when they were exposed to 6:2 FTCA (mutant # 15, 32 and 38 – Table S2). The disruption of the genetic locus in all 3 non-defluorinating mutants was identified coding for a putative MhPC superfamily protein. The MhPC superfamily of proteins is known to harbor other proteins such as fluoroacetate dehalogenase (UniProt - Q6NAM1) that are capable of –C-F bond cleavage. This identified gene was cloned into the heterologous expression host <em>M. smegmatis</em> MC²-155. After induction, the <em>M. smegmatis</em> MC²-155 transformant exhibited the ability to defluorinate 6:2 FTCA at a rate of 13 µmol/h (V_max = 80.9 µmol/min and K_m = 5.04 mM in Michaelis-Menten models). In contrast, defluorination was not observed in either abiotic or biotic controls. Further characterization of the novel defluorinase indicated that it could moderately defluorinate the unsaturated PFAS compound 6:2 FTCUA (4.9 µmol/h fluoride) and minimally defluorinate 5:2 sFTOH (1.3 µmol/h fluoride). The novel defluorinase indicated a maximal specific activity of 12.9 ± 1.9 µmol F/hr/g protein, against its primary PFAS substrate, 6:2 FTCA. However, it showed no activity with 5:3 FTCA or sulfonated PFAS compounds such as 6:2 FTS and 8:2 FTS. The wild-type <em>Rhodococcus</em> could defluorinate 6:2 FTCA at a rate of 2.2 µmol/h. The discovery of this MhPC class novel defluorinase in WT <em>R</em>.<em>jostii</em> RHA1. has substantial value since it is responsible for the critical step that initiates defluorination of PFAS compounds such as 6:2 FTCA.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110724"},"PeriodicalIF":3.4,"publicationDate":"2025-07-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144702367","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}