Enzyme and Microbial Technology最新文献

{"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":"2025-10-01","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":"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":"2025-10-01","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":"Comparison of novel α-glucosidases in glycoside hydrolase family 97 isolated from Bacteroides thetaiotaomicron","authors":"Dam-Seul Ko ,&nbsp;Hyun-Mo Jeong ,&nbsp;Yu-Jeong Shin,&nbsp;Da-Woon Jeong,&nbsp;Na-Ri Kim,&nbsp;Jae-Hoon Shim","doi":"10.1016/j.enzmictec.2025.110696","DOIUrl":"10.1016/j.enzmictec.2025.110696","url":null,"abstract":"<div><div>In this study, three genes encoding novel Glycoside Hydrolase (GH) 97 enzymes were cloned from <em>Bacteroides thetaiotaomicron</em> and expressed in <em>Escherichia coli</em>. The recombinant enzymes (Bt_4581, Bt_0683, Bt_3163) were purified using Ni-NTA affinity chromatography and subsequently characterized. All three enzymes released glucose from the non-reducing ends of oligosaccharides and displayed metal ion dependency. Among them, Bt_4581 hydrolyzed a wide range of α-glycosidic linkages, while Bt_0683 and Bt_3163 showed narrower substrate specificity. Amino acid sequence analysis indicated that Bt_4581 and Bt_0683 belong to Group 1, whereas Bt_3163 is part of Group 3. Kinetic studies revealed that Bt_4581 preferred maltooligosaccharides with an odd number of glucosyl units. In contrast, Bt_3163 exhibited a preference for α-<em>p</em>NPG, confirming it as the first characterized α-glucosidase in Group 3 of the GH 97 family.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110696"},"PeriodicalIF":3.4,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144522232","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":"Crystal structure of cyclohexylamine oxidase from Acinetobacter sp. YT−02 reveals key residues for catalytic activity and substrate specificity","authors":"Jing Wu ,&nbsp;Zhenggang Han ,&nbsp;Pengrong Li ,&nbsp;Jing Li ,&nbsp;Yuanyuan Chen ,&nbsp;Shangbo Ning ,&nbsp;Hong-jun Chao ,&nbsp;Xue-wang Gao ,&nbsp;Dazhong Yan","doi":"10.1016/j.enzmictec.2025.110700","DOIUrl":"10.1016/j.enzmictec.2025.110700","url":null,"abstract":"<div><div>Cyclohexylamine oxidase is a member of amine oxidases that catalyzes the conversion of cyclohexylamine to cyclohexanone. In our previous work, the enzymatic activity assay of cyclohexylamine oxidase CHAO_YT-02 indicated that its specific activity towards cyclohexylamine of CHAO_YT-02 was ten times higher than that of its homolog CHAO_IH-35A. In this study, the crystal structure of CHAO_YT-02 was determined by the molecular replacement method at a resolution of 1.49 Å. The atomic structure revealed that the amino acid residues Leu302, Trp70, Phe197, Phe349, and Tyr440 constitute the active center pocket of the enzyme. Amino acid residues Ile180, Leu181, and Trp332 separate the active center pocket and an intermediate pocket. Moreover, a molecular dynamics (MD) simulation and the calculation of the binding free energy were performed to predict substrate entry and product release from cyclohexylamine oxidases. Single-amino acid substitution mutants (W70A, I180A, L181A, I208A, F197A, L302A, W332A, F349A, and Y440A) of CHAO_YT-02 were constructed to investigate the role of these amino acid residues in enzymatic properties and substrate specificity. The results indicated that both the amino acid residues in the active center pocket and gating the two pockets affected the activity or substrate specificity of CHAO_YT-02. This study on the structure and catalytic mechanism of cyclohexylamine oxidase is beneficial to eliminating toxic amine compounds in the environment.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110700"},"PeriodicalIF":3.4,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144549870","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":"Arazyme prevents skin aging through regulation of matrix metalloproteinase and collagen synthesis","authors":"Jong-Hoon Kim ,&nbsp;Hwa Lee ,&nbsp;Kwang-Hee Son ,&nbsp;Tae-Sook Jeong ,&nbsp;Ho-Yong Park","doi":"10.1016/j.enzmictec.2025.110695","DOIUrl":"10.1016/j.enzmictec.2025.110695","url":null,"abstract":"<div><div>Arazyme, an enzyme derived from <em>Serratia proteamaculans</em>, has demonstrated efficacy in enhancing skin barrier function in studies involving skin cell treatments and topical application on animal skin. The objective of this study was to assess the anti-wrinkle and anti-aging effects of Arazyme in skin keratinocytes and fibroblasts subjected to ultraviolet B (UVB) radiation and oxidative stress. Keratinocytes (HaCaT cells) and fibroblasts (CCD-986sk) were exposed to UVB (15 mJ/cm²) radiation or oxidative stress induced by 2 mM 2,2′-azobis(2-amidinopropane) dihydrochloride (AAPH), followed by treatment with Arazyme (0.1–0.5 μM) for 24 h. The effects of Arazyme were compared to those of individual treatments with papain, trypsin, or retinol, which served as reference compounds. Key parameters examined included the expression of matrix metalloproteinases (<em>MMP-1, MMP-3, and MMP-13</em>), collagen synthesis, and cellular senescence markers (<em>LMNB1, p16, p21</em>, and <em>p53</em>). Additionally, the impact of Arazyme on cellular signaling pathways, including ERK, JNK, and NF-κB, was assessed. Arazyme significantly suppressed UVB-induced expression of MMP-1, MMP-3, and MMP-13 in a dose-dependent manner in HaCaT cells compared to other treatments. In UVB-exposed fibroblasts, Arazyme reduced both mRNA and protein levels of MMPs, while also enhancing procollagen concentration and collagen gene expression. Furthermore, Arazyme inhibited the activation of ERK, JNK, and NF-κB signaling pathways in keratinocytes. In AAPH-stimulated HaCaT cells, Arazyme significantly attenuated the expression of senescence-related markers, including <em>LMNB1, p16, p21</em>, and <em>p53</em>, and decreased the proportion of senescence-positive cells in fibroblasts. Our in vitro findings suggest that Arazyme may help attenuate UVB- and oxidative stress-induced markers of skin aging, indicating its potential as a candidate for further investigation in anti-aging skincare research.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110695"},"PeriodicalIF":3.4,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144321341","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":"2025-10-01","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":"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":"2025-10-01","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}

{"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":"2025-10-01","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":"Efficient isoprimeverose production using an enzyme cocktail from engineered Aspergillus oryzae and yeast-assisted purification","authors":"Satoshi Wakai ,&nbsp;Nanami Nakashima ,&nbsp;Hiroko Tsutsumi ,&nbsp;Yoji Hata ,&nbsp;Fahmi Baihaqqi ,&nbsp;Akihiko Kondo ,&nbsp;Chiaki Ogino","doi":"10.1016/j.enzmictec.2025.110698","DOIUrl":"10.1016/j.enzmictec.2025.110698","url":null,"abstract":"<div><div><em>Aspergillus oryzae</em> is a filamentous fungus that possesses various types of carbohydrate -degrading enzymes. Among these, isoprimeverose-producing enzyme (IpeA), acts on a key component of the plant cell wall structure, xyloglucan, to catalyze the release of isoprimeverose — a rare disaccharide that is expected to possess valuable prebiotics properties. Despite these expectations, however, a process for the effective production of isoprimeverose from the xyloglucan still requires further development for commercial-level application. A complicating factor for the lack of such a valuable process is that plant-derived xyloglucan is often modified with other sugars such as galactose and arabinose. Therefore, the effective production of isoprimeverose requires a cooperative form of degradation that must utilize different enzymes. In this study, we genetically engineered two <em>A. oryzae</em> strains — one produces IpeA and the other produces endoglucanase. The two strains were cultivated separately, and an enzyme cocktail was prepared using their respective culture supernatants. This enzyme cocktail successfully produced isoprimeverose from tamarind xyloglucan and tamarind seed gum. Approximately 14 g/L of isoprimeverose was obtained, which corresponds to a theoretical conversion rate of over 90 %. Although glucose and galactose remained in the reaction solution after enzymatic degradation, these by-products could be easily removed via treatment with <em>Saccharomyces cerevisiae</em>. Our developed process, which mimics traditional Japanese sake fermentation using <em>A. oryzae</em> and <em>S. cerevisiae</em>, has enabled efficient production of isoprimeverose.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110698"},"PeriodicalIF":3.4,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144330453","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":"The effect of the cspA gene on growth development and butenyl-spinosyn biosynthesis in Saccharopolyspora pogona","authors":"Duo Jin,&nbsp;Shanrui Wang,&nbsp;Wangqiong Chen,&nbsp;Jing Fang,&nbsp;Jie Rang,&nbsp;Liqiu Xia,&nbsp;zirong zhu","doi":"10.1016/j.enzmictec.2025.110701","DOIUrl":"10.1016/j.enzmictec.2025.110701","url":null,"abstract":"<div><div>Cold shock proteins (CSPs) represent a universal class of proteins in microorganisms, rapidly inducible under low temperature conditions. As molecular chaperones for RNA, they bind to single-stranded nucleotides, preventing the formation of complex secondary structures. This facilitates efficient translation and gene expression regulation. This investigation pioneers the study of the <em>cspA</em> gene through metabolic engineering techniques, to uncover its critical biological roles in the growth and development of <em>Saccharopolyspora pogona</em> and in butenyl-spinosyn biosynthesis. Employing comparative proteomic and targeted metabolomic analyses, this research elucidates the metabolic pathway alterations prompted by the augmented presence of the cold shock protein CspA. Additionally, it offers initial insights into the regulatory mechanisms by which CspA affects <em>S. pogona</em>'s growth, development, and butenyl-spinosyn production. The outcomes of this study significantly advance our theoretical understanding of the rational optimization of butenyl-spinosyn biosynthetic pathways. They also provide valuable guidance for other actinobacteria aiming to boost their resilience to harsh environments by overexpressing the <em>cspA</em> gene.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"190 ","pages":"Article 110701"},"PeriodicalIF":3.4,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144471575","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}