Enzyme and Microbial Technology最新文献

{"title":"Exploring the role of catalytic triad Ser-His-Asp on the dynamics of the Lactobacillus helveticus cell-envelope proteinases","authors":"Li Chen ,&nbsp;Ni Lei ,&nbsp;Guanli Du ,&nbsp;He Chen ,&nbsp;Guowei Shu","doi":"10.1016/j.enzmictec.2025.110723","DOIUrl":"10.1016/j.enzmictec.2025.110723","url":null,"abstract":"<div><div>Lactic acid bacterium (LAB) hydrolyzes milk proteins into small bioactive peptides to flourish milk nutrition value. Cell-envelope proteinases (CEPs) are vitally important to bacterial growth, the texture and flavor formation, and the generation of bioactive peptides in fermented milk. Previous literature suggested PR domain of CEP was responsible for the catalytic activity. This study aims to explore the CEP molecular mechanism by delineating the catalytic triad Ser-His-Asp active sites of PR domain in <em>Lactobacillus helveticus</em> CNRZ32 with the aid of homology modeling, molecular docking and dynamics analysis. These results proved that catalytic triads were involved in the PR activation and the catalytic residues Ser608 and His270 appeared to be the core of catalytic process. Our study gained novel insights on the catalytic mechanism of CEP of <em>L. helveticus</em> CNRZ32 which would be a pioneer to facilitate the development of dairy product industry.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110723"},"PeriodicalIF":3.4,"publicationDate":"2025-07-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144679800","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":"Modulating UDP-glucuronosyltransferase activity: Mechanisms, clinical implications, therapeutic strategies, and future directions in drug development","authors":"Ahmed A. Allam ,&nbsp;Hassan A. Rudayni ,&nbsp;Noha A. Ahmed ,&nbsp;Faris F. Aba Alkhayl ,&nbsp;Al Mokhtar Lamsabhi ,&nbsp;Emadeldin M. Kamel","doi":"10.1016/j.enzmictec.2025.110711","DOIUrl":"10.1016/j.enzmictec.2025.110711","url":null,"abstract":"<div><div>UDP-glucuronosyltransferases (UGTs) are essential enzymes in the phase II metabolism of endogenous and exogenous compounds, playing a critical role in detoxification, drug metabolism, and clearance. Their function is crucial for the pharmacokinetics of numerous therapeutic agents, but UGT inhibition can result in altered drug metabolism, increased toxicity, or reduced efficacy. This review explores the mechanisms of UGT inhibition, its implications for drug metabolism and pharmacokinetics, and the clinical relevance of such inhibition in the context of drug-drug interactions (DDIs). We discuss the therapeutic strategies targeting UGTs, the impact of environmental and dietary factors on UGT activity, and the role of pharmacogenetics in modulating UGT function. Moreover, the review highlights the role of UGTs in xenobiotic detoxification and addresses the challenges in identifying and modulating UGT inhibition in drug development. Finally, we identify future research directions for understanding UGT inhibition and its clinical applications. By synthesizing recent advances in the field, this review provides a comprehensive overview of the dynamic role of UGTs in drug metabolism, offering insights for optimizing drug therapy and minimizing adverse interactions.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110711"},"PeriodicalIF":3.4,"publicationDate":"2025-07-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144595702","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":"Ovomucoid hydrolysates produced by pepsin stimulate immune activity of RAW 264.7 macrophages via the MAPK/NF-κB pathway","authors":"Seung-Woo Yu ,&nbsp;Hyeong-Jin Kim ,&nbsp;Jin-Hong Jang ,&nbsp;Kee-Tae Kim ,&nbsp;Dong Uk Ahn ,&nbsp;Hyun-Dong Paik","doi":"10.1016/j.enzmictec.2025.110710","DOIUrl":"10.1016/j.enzmictec.2025.110710","url":null,"abstract":"<div><div>Ovomucoid (OVM) was hydrolyzed by proteolytic enzymes to increase immune-enhancing effects for health. Bromelain, Neutrase®, papain, and pepsin were used to hydrolysis and immunostimulatory properties of OVM hydrolysates were evaluated in RAW 264.7 macrophages in this study. Among the OVM hydrolysates, pepsin hydrolysate (OMPH) produced peptides with 10–20 kDa molecular weight, as confirmed by SDS-PAGE. In RAW 264.7 macrophages, OVM hydrolysates at 500 μg/mL or less exhibited high cell viability, exceeding 80 %. In the Griess assay, OMPH produced higher levels of nitric oxide (NO) compared to other OVM hydrolysates. Additionally, OMPH upregulated inducible nitric oxide synthase (iNOS) mRNA expression in a concentration-dependent manner. Similarly, the expression of TNF-α and IL-6 was increased by OMPH. Furthermore, OMPH activated mitogen-activated protein kinase (MAPK) and nuclear factor kappa B (NF-κB), with increased phosphorylation of p38, JNK, ERK, p65, and IκB-α, in particular exhibiting high ERK and IκB-α phosphorylation levels. Furthermore, RAW 264.7 macrophages treated with OMPH exhibited an enlarged cell morphology and a dendritic-like shape compared to the control. Finally, liquid chromatography-tandem mass spectrometry (LC-MS/MS) fractionation of OMPH identified nine peptides, including the EGKDVLVCNK, which was determined to be immunostimulatory properties. These results suggest that OMPH can be used as a natural bio-functional ingredient for potential enhancing human immunity in both the functional food and pharmaceutical industries.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110710"},"PeriodicalIF":3.4,"publicationDate":"2025-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144595703","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":"Functional characterization of a Stevia rebaudiana flavonoid glycosyltransferase","authors":"Chen-Xin Guo ,&nbsp;Jiyan Li ,&nbsp;Yu Wang ,&nbsp;Tang Li ,&nbsp;Heng Yin","doi":"10.1016/j.enzmictec.2025.110708","DOIUrl":"10.1016/j.enzmictec.2025.110708","url":null,"abstract":"<div><div><em>Stevia rebaudiana</em>, a perennial herb, is recognized not only for its sweet steviol glycosides but also for its rich flavonoid content, which confer pharmacological properties including anti-inflammatory, antimicrobial, and anticancer activities. However, the enzymatic basis underlying flavonoid modification in <em>S. rebaudiana</em> remains poorly understood. In this study, we identified, cloned, and heterologously expressed a novel flavonoid glycosyltransferase gene, SrUGT72B1 in <em>E. coli</em>. The recombinant SrUGT72B1 catalyzed the glycosylation of multiple flavonoids using UDP-glucose as the primary sugar donor, and exhibited broad substrate promiscuity toward apigenin, luteolin, phloretin and kaempferol. In addition to UDP-glucose, SrUGT72B1 also accepted UDP-xylose and UDP-rhamnose, with UDP-glucose exhibiting the highest catalytic efficiency. Biochemical characterization revealed that the enzyme functions optimally at pH 9.0 and 50 °C. Notably, SrUGT72B1 demonstrates regioselective 5-O-glycosylation toward apigenin, a rare activity among plant glycosyltransferases. Molecular docking and molecular dynamics simulations provided structural insights into this unique regioselectivity and substrate recognition. Together, these findings establish SrUGT72B1 as a previously uncharacterized flavonoid 5-O-glycosyltransferase, expanding the functional landscape of plant UGTs and offering potential applications in the biosynthesis of value-added flavonoid glycosides.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110708"},"PeriodicalIF":3.4,"publicationDate":"2025-07-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144589058","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":"Improved total carotenoid content from Planococcus plakortidis NIOT3 through microwave assisted extraction and genome-guided pathway annotation","authors":"Nishanthika Thenmozhi Kulasekaran,&nbsp;Mary Leema J T,&nbsp;Vishal Vasavan M V,&nbsp;Dharani Gopal,&nbsp;Jeya Marimuthu","doi":"10.1016/j.enzmictec.2025.110707","DOIUrl":"10.1016/j.enzmictec.2025.110707","url":null,"abstract":"<div><div>With an increasing demand for natural colorants, marine microbes have become attractive targets for novel natural colorants like carotenoids. Microbial carotenoid extraction by green approach is advantageous over traditional methods which minimize energy usage and reduce extraction time. In the current study, an orange pigmented marine bacterium <em>Planococcus plakortidis</em> NIOT3 was isolated from the Sesostris bank of Arabian Sea and found to produce desirable level of total carotenoids (320 ± 24 µg/g DW) when grown in rich medium. An energy efficient green approach using Microwave Assisted Extraction was evaluated for carotenoid yield by one factor and statistical optimization of the MAE process conditions including exposure time, alkali concentration and Solid:Liquid ratio which resulted in a 3.26 fold increase in total carotenoid content of 2835 ± 152 µg/g DW. Genome sequencing and annotation revealed genes that are involved in C30 carotenoid biosynthesis. C30 carotenoids like glycosylated diapolycopene and methyl-5-glucosyl-5,6-dihydro-apo-4,4’-lycopenoate produced by NIOT3 were identified by LC-MS analyses as major products. Additionally, LC-MS analysis revealed a minor product with a molecular weight of <em>m/z</em> of 568.84 which corresponds to zeaxanthin, a C40 carotenoid. The study highlights the biotechnological potential of <em>P. plakortidis</em> in carotenoid production.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110707"},"PeriodicalIF":3.4,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144570332","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":"Functional characterization of CEL3C reveals its critical role in regulating cellulase gene expression in Trichoderma reesei Rut C30","authors":"Lu Wang ,&nbsp;Xiao He ,&nbsp;Tian Tian ,&nbsp;Jian Cheng ,&nbsp;Ruolan Cao ,&nbsp;Jie Hou ,&nbsp;Hui Lin ,&nbsp;Yonghao Li","doi":"10.1016/j.enzmictec.2025.110706","DOIUrl":"10.1016/j.enzmictec.2025.110706","url":null,"abstract":"<div><div>The nuclear-localized β-glucosidase CEL3C in <em>Trichoderma reesei</em> plays a pivotal role in cellulase regulation, though its mechanism remains poorly understood. To address this, we disrupted CEL3C in the hypercellulolytic strain <em>T. reesei</em> Rut C30 via CRISPR-Cas9 and evaluated cellulase production under sophorose-rich MGD induction. Deletion of CEL3C significantly enhanced total cellulase activity by 31.28 % (<em>p</em> &lt; 0.05), with β-glucosidase, endoglucanase, and cellobiohydrolase activities increasing by 94.97 %, 19.40 %, and 28.99 %, respectively. These improvements were driven by transcriptional upregulation of core cellulase genes (CEL7A: 2.01-fold; CEL6A: 1.5-fold; CEL12A: 2.0-fold; CEL5A: 1.32-fold) and β-glucosidases (CEL3A: 6.41-fold; CEL3B: 5.02-fold), confirming transcriptional-level control as the dominant regulatory mechanism. Transcriptomic profiling identified 688 differentially expressed genes (399 upregulated, 299 downregulated), with key changes including activation of transcriptional activators XYR1 (59.6 % increase), ACE3 (75.49 % increase), and RXE1 (161.56 % increase), suppression of repressors RCE1 (65.86 % decrease) and RCE2 (65.23 % decrease), and induction of sugar transporters (TrireC30_133589: 13.41-fold) and ER chaperones (BIP1: 1.26-fold; PDI1: 1.55-fold). These alterations collectively enhanced inducer uptake, enzyme maturation, and secretion while alleviating MAPK-mediated repression (TMK2: 110.54 % decrease). Intracellular sugar profiling revealed that gentiobiose and cellobiose were undetectable in the <em>T. reesei</em> ΔCEL3C, whereas glucose and sophorose levels increased by 31.71 % and 13.45 % (<em>p</em> &lt; 0.05), respectively. These results suggest that CEL3C deletion enhances β-glucosidase-mediated hydrolysis of disaccharides into glucose and possibly promotes sophorose formation via transglycosylation. In parallel, the upregulation of disaccharide transporters may facilitate sophorose uptake. Together, these two mechanisms contributed to the intracellular enrichment of sophorose, thereby amplifying cellulase gene induction and enzyme production. Our findings establish CEL3C as a dual-function nuclear regulator that balances cellulase synthesis through transcriptional and enzymatic pathways, providing actionable targets for engineering <em>T. reesei</em> with optimized industrial cellulase yields.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110706"},"PeriodicalIF":3.4,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144549872","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":"Structural determinants of unique substrate specificity of d-amino acid oxidase of the thermophilic fungus Rasamsonia emersonii","authors":"Yuya Shimekake,&nbsp;Takehiro Furuichi,&nbsp;Daiki Imanishi,&nbsp;Shouji Takahashi","doi":"10.1016/j.enzmictec.2025.110705","DOIUrl":"10.1016/j.enzmictec.2025.110705","url":null,"abstract":"<div><div><span>d</span>-Amino acid oxidase from the thermophilic fungus <em>Rasamsonia emersonii</em> (<em>Re</em>DAAO) has garnered attention due to its high stability and broad substrate specificity, making it a promising candidate for various applications. In this study, we explored the structural factors underlying the unique substrate specificity of <em>Re</em>DAAO, particularly its broad substrate range and <span>d</span>-Glu oxidation ability. Comparing <em>Re</em>DAAO with <em>Td</em>DAAO—a homologous <span>d</span>-amino acid oxidase from the thermophilic fungus <em>Thermomyces dupontii</em>—revealed that <em>Re</em>DAAO lacks the YVLQG loop present in <em>Td</em>DAAO, which exhibited narrower substrate specificity. Inserting the YVLQG loop into <em>Re</em>DAAO narrowed its substrate specificity to match <em>Td</em>DAAO, while deleting the sequence from <em>Td</em>DAAO broadened its substrate specificity, resembling <em>Re</em>DAAO. A <em>Td</em>DAAO structural model suggests that the YVLQG loop could interact with a spatially adjacent region covering the active site, distinct from the canonical active-site lid in DAAOs, creating steric hindrance that limits access to the catalytic pocket. Additionally, the unexpected activity of <em>Re</em>DAAO toward <span>d</span>-Glu appears to depend on Arg97 and Ser231, which could interact with <span>d</span>-Glu side chain. Alanine substitutions at these residues significantly reduced <span>d</span>-Glu activity, revealing that Arg97 is essential for catalytic turnover while Ser231 is critical for substrate binding. Together, these results suggest that the YVLQG loop together with the spatially adjacent region acts as a steric gate that modulates access to the catalytic pocket, and Arg97/Ser231 plays an important role in <span>d</span>-Glu. These findings deepen our understanding of the structure–function relationship of DAAO and provide a foundation for developing improved DAAO variants for industrial applications.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110705"},"PeriodicalIF":3.4,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144557435","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":"Optimization of physico-chemical parameters for synergistic production of xylano-cellulolytic enzymes by novel Pantoea sp. (PQ584882) under solid-state fermentation using statistical design approach","authors":"Neha Maurya ,&nbsp;Harsh Sable ,&nbsp;Jyoti Chauhan ,&nbsp;Amit Kumar ,&nbsp;Sharad Agrawal","doi":"10.1016/j.enzmictec.2025.110697","DOIUrl":"10.1016/j.enzmictec.2025.110697","url":null,"abstract":"<div><div>Xylanase and cellulase have become increasingly significant due to their versatile applications in the food, paper, biofuel, and pharmaceutical industries. Nevertheless, the current production of these enzymes relies on costly substrates, with estimates indicating that over 30 % of the production expenses are attributed to these substrates. The objective of this study is to optimize the physicochemical parameters for obtaining the maximum production of xylanase &amp; cellulase enzyme from <em>Pantoea sp.</em> (PQ584882). The production conditions were statistically optimized using Plackett-Burman design (PBD) and Central Composite design (CCD). The significant variables identified through PB design including temperature, substrate-to-moisture ratio, K₂HPO₄, peptone, surfactant, inoculum size, inoculum age, incubation time, and pH were further optimized using the CCD approach. This optimization process revealed the most influential factors affecting xylanase &amp; cellulase production, with optimal conditions observed at a temperature of 40◦C, Moisture Proportion, 15 mL; K₂HPO₄ 6 mM; peptone, 1.55 %; Castor oil 0.5 %; inoculum size, 1.55 % (v/w); inoculum age, 18 h; an incubation time, 87 h. The optimized CCD model displayed a 1.84-fold greater xylanase &amp; cellulose production than the PB design approach. These findings suggest that wheat bran, a readily available agro-waste, could be a feasible alternative to the conventional substrate, beechwood xylan and CMC (Carboxy methyl cellulose) for the production of xylanase &amp; cellulase enzymes with the possibility of achieving higher production levels optimized by using a statistical design approach<strong>.</strong></div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110697"},"PeriodicalIF":3.4,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144489382","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":"Glycosylation of terpenes with a substrate-flexible recombinant glycosyltransferase from Micromonospora inoyensis NRRL 3292","authors":"Mingyu Yeo ,&nbsp;Bohyun Choi ,&nbsp;Hong Ji Im ,&nbsp;Jiwon Na ,&nbsp;Siyeon Choi ,&nbsp;Hyunsung So ,&nbsp;Je Won Park","doi":"10.1016/j.enzmictec.2025.110704","DOIUrl":"10.1016/j.enzmictec.2025.110704","url":null,"abstract":"<div><div>Glycosyltransferase (GT)-specific degenerate PCR screening of the established fosmid libraries of the soil actinomycete <em>Micromonospora inoyensis</em> NRRL 3292, followed by <em>in silico</em> sequencing of target clones, allowed us to isolate members of the family 1 GT-encoding gene. A recombinant MiTGT, as a His-tagged protein, was heterologously expressed in <em>Escherichia coli</em>. Its bio-catalytic reactions with both natural terpene aglycones derived from natural sweeteners including stevioside and mogroside (as glycosyl acceptors) and nucleotide-activated hexoses (as glycosyl donors) created a number of structurally diversified terpene glycosides, thus characterizing MiTGT as a terpene glycosyltransferase with substrate-flexibility. Chromatographic isolation of the product glycosides followed by the instrumental analyses, clearly confirmed the previously unprecedented stereospecific glycosides as steviol-13-<em>O</em>-α-glucoside, steviol-13-<em>O</em>-α-(2′-deoxy)glucoside and steviol-13-<em>O</em>-α-galactoside, mogrol-3-<em>O</em>-α-glucoside, mogrol-3-<em>O</em>-α-(2′-deoxy)glucoside, mogrol-3-<em>O</em>-α-galactoside. Moreover, their elastase inhibitory activities together with anti-proliferative activities against the human pancreatic adenocarcinoma cell line PANC-1 were further investigated, hence representing the cosmeceutical and pharmaceutical potentials of the designated terpene glycosides. This is the first report on the microbe-origin bio-catalytic production of unnatural terpene α-configured glycosides.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110704"},"PeriodicalIF":3.4,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144502061","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":"Microbial community dynamics and functional potential during the natural fermentation of rose: A metagenomic and volatile compound analysis","authors":"Zhiyuan Yin,&nbsp;Kangdi Cao,&nbsp;Ningfei Duan,&nbsp;Zhiguo Zhang","doi":"10.1016/j.enzmictec.2025.110703","DOIUrl":"10.1016/j.enzmictec.2025.110703","url":null,"abstract":"<div><div>This study investigates the dynamics of microbial communities and their functional characteristics during the natural fermentation of roses. Utilizing metagenomic sequencing and volatile compound analysis, the research elucidates the succession of microbial communities and their relationship with the flavor compound production. The findings indicate that <em>Klebsiella</em> and <em>Pichia</em> are predominant in the early stages of fermentation, while <em>Acetobacter</em> and <em>Cyberlindnera</em> become more abundant in the middle and later stages. The glycosyltransferase (GT) family is identified as the primary carbohydrate-active enzyme (CAZy) family involved in fermentation, with GT1 and GT2 exhibiting a higher gene abundance. Functional genes are predominantly associated with the carbohydrate and amino acid metabolism. Analysis of volatile compounds reveals that substances such as phenethyl acetate and (S,S)-2,3-Butanediol are closely related to the structure of the microbial community. These findings contribute to a deeper understanding of the mechanisms underlying rose fermentation and offer a theoretical foundation for technological advancements in the rose product industry.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110703"},"PeriodicalIF":3.4,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144481156","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}