Enzyme and Microbial Technology最新文献

{"title":"An integrated approach based on sequential fractionation and specific enzymatic saccharification of green algae Ulva sp. biomass","authors":"Nesrine Ben Yahmed ,&nbsp;Rahma Masmoudi ,&nbsp;Emna Ben Yahmed ,&nbsp;Cyrine Ben Amor ,&nbsp;Issam Smaali","doi":"10.1016/j.enzmictec.2025.110715","DOIUrl":"10.1016/j.enzmictec.2025.110715","url":null,"abstract":"<div><div>Marine green algae of the <em>genus Ulva</em> are abundant worldwide. In the case of eutrophication, they can be stranded in large quantities, thereby causing ecological and economic problems. Compared to other macroalgae, this biomass remains underexploited on an industrial scale. Thus, the aim of this study was to develop an integrated downstream process applicable to the biomass of the green algae <em>Ulva</em> sp., allowing a major sequential recovery of high-added-value fractions corresponding to pigments, ulvan, alkali-soluble hemicelluloses, and cellulose. Indeed, the proposed concept using cascade extractions enable to produce 0.64 ± 0.16 % of pigments rich in chlorophylls and caroténoids, 28 ± 0.8 % of ulvan, 5 ± 0.3 % of alkali-soluble hemicelluloses and 10 ± 0.4 % of cellulose based on initial dry weight. Characterization of the extracted polysaccharides and verification of their purity were confirmed using FTIR and monosaccharide composition analyses. To better evaluate the biodegradability and the success of the extraction procedure, enzymatic saccharification was applied at the end of the cascade using the cellulose fraction as the substrate. In parallel, saccharification of the total algal biomass was also carried out under the same conditions. Results showed a significant improvement in conversion yields from 74.6 ± 0.85 % to 84 ± 0.7 % showing that <em>Ulva</em>’s cellulose fraction can be a promising candidate for biofuels production. This study presents a sustainable biorefinery approach that allows almost complete fractionation and bioconversion of green macroalgae, and integrates the concept of a circular bio-economy.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110715"},"PeriodicalIF":3.4,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144696931","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":"2025-12-01","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":"Enhanced production of hyperthermophilic Pyrococcus furiosus β-glucosidase in Corynebacterium glutamicum by optimization of the promoter, vector backbone, and His-tag location","authors":"Mehmet Emre Erkanli ,&nbsp;Ryu Hong Park ,&nbsp;Jingwei Liu ,&nbsp;Gunhyeong Lee ,&nbsp;Amulya Hota ,&nbsp;Jehyeon Lee ,&nbsp;Chaehyun Ryu ,&nbsp;Ki Jun Jeong ,&nbsp;Jin Ryoun Kim","doi":"10.1016/j.enzmictec.2025.110725","DOIUrl":"10.1016/j.enzmictec.2025.110725","url":null,"abstract":"<div><div>A hyperthermophilic β-glucosidase from <em>Pyrococcus furiosus</em> (PfBGL) is a highly stable and active glycoside hydrolase, well-suited for a wide range of applications. Although PfBGL has been successfully expressed in <em>Escherichia coli</em>, the use of this host limits its applicability in the healthcare and food processing industries due to safety concerns associated with <em>E. coli</em>-based expression systems. Recently, <em>Corynebacterium glutamicum</em> has emerged as a safe and versatile microbial platform for the expression of recombinant proteins used in food processing, pharmaceutical development, therapeutic enzyme production, and probiotic applications. Despite these advantages, heterologous expression in <em>C. glutamicum</em> is often hindered by low protein yields, and PfBGL expression in this host has not been previously explored. In this study, we report for the first time the production of PfBGL in <em>C. glutamicum</em>, achieving a 15-fold enhancement through the optimization of the promoter, the vector backbone, and the His-tag location. Among four different promoters, the <em>P</em>_trc promoter with <em>RBS</em>_T7 yielded the highest PfBGL expression. For the <em>P</em>_trc-<em>RBS</em>_T7 combination, the PfBGL expression levels further varied depending on the vector backbone. Interestingly, placing the His-tag at the N-terminus of PfBGL not only increased its expression in <em>C. glutamicum</em>, but also enhanced its enzymatic activity (<em>k</em>_cat/<em>K</em>_m), when compared to C-terminal tagging. Overall, this study showcases a simple yet effective strategy at both genetic and protein levels to enhance PfBGL production in <em>C. glutamicum</em>, thereby broadening its utility as a host for diverse protein production applications.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110725"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144724365","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":"2025-12-01","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":"Mechanism of static magnetic field influencing morphogenesis of Flavobacterium sp. m1-14","authors":"Mengxue Zhang ,&nbsp;Peng Wang ,&nbsp;Han Wang ,&nbsp;Li Wang ,&nbsp;Xiumin Ding ,&nbsp;Zhiming Zheng ,&nbsp;Genhai Zhao","doi":"10.1016/j.enzmictec.2025.110714","DOIUrl":"10.1016/j.enzmictec.2025.110714","url":null,"abstract":"<div><div>The biological effects of static magnetic fields (SMF) have long been a research hotspot in academia. While the impact of magnetic fields on microbial morphogenesis is closely linked to microbial fermentation efficiency, the specific mechanism remains incompletely elucidated. In this study, the vitamin K₂-producing strain <em>Flavobacterium sp</em>. m1–14 was exposed to a static magnetic field of up to 9 Tesla (T) for 24 h. It was observed that the bacterial cells shrank, showing an overall decreasing trend in size. The length, width, and aspect ratio decreased by approximately 25.27 %, 14.28 %, and 17.95 %, respectively. Furthermore, the physiological and biochemical properties of the bacteria underwent significant changes. Specifically, the cell membrane permeability increased by approximately 6.2 %; the activities of Na⁺-K⁺-ATPase and Ca²⁺-Mg²⁺-ATPase decreased by about 57.5 % and 34.7 %, respectively; and the membrane potential decreased significantly. In addition, intracellular ATP levels decreased by approximately 12 %, a change directly attributed to impaired ATP metabolism. Investigations into the key morphological regulatory genes <em>mreB</em> and <em>ftsZ</em> revealed that their transcription levels were unregulated by 190 % and 38 %, respectively—likely a stress response induced by cellular energy deficiency. Under conditions of high <em>mreB</em> and <em>ftsZ</em> expression, cells reduce their size to minimize metabolic loss, thereby adapting to extreme environments.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110714"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144720775","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":"2025-12-01","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":"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":"2025-12-01","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":"Developing a urea biosensor and safe blood cleaning method utilizing a novel high throughput La-doped CeO2 nanosized artificial urease with high biocompatibility and enzyme-like activity","authors":"Naushad Ahmad ,&nbsp;Ashok Kumar Bishoyi ,&nbsp;Suhas Ballal ,&nbsp;Aman Shankhyan ,&nbsp;Shaker Al-Hasnaawei ,&nbsp;Karthikeyan Jayabalan ,&nbsp;Laxmidhar Maharana ,&nbsp;Madan Lal","doi":"10.1016/j.enzmictec.2025.110736","DOIUrl":"10.1016/j.enzmictec.2025.110736","url":null,"abstract":"<div><div>Herein, a urea biosensor and safe blood cleaning method utilizing a novel high throughput La-doped CeO₂ nanosized artificial urease with high biocompatibility and enzyme-like activity were developed. The urease-like activity, stability composition, morphological characteristics, size, biocompatibility, and crystalline characteristics of the artificial urease were assessed. Considering its high urease-like activity, it is applied for both urea biosensing and safe blood cleaning. The effective factors on the sensing conditions were optimized, providing a wide linear range over 1–10 µM and a low detection limit of 0.5 µM. The repeatability and reproducibility assessments revealed a %RSD of 1.7 % and 2.7 %, in order. The selectivity studies and real blood analysis revealed highly selective, accurate, and reliable determination of urea in biosamples using the developed method, providing a %recovery of 97.8–99.5 % with a low %RSD range of 1.4–3.3 %. Besides, the safe blood cleaning experiments were also performed by urea mineralization from blood. The results exhibited a high blood cleaning yield of 99.5 % at a short time of 30 min, revealing 1.8-fold higher cleaning efficiency for the artificial urease compared to native urease. The reusability studies showed that the blood cleaning yield was saved for about 10 cycles and then it decreased by increasing the operational cycles, reaching 78.6 % after 17 cycles. The shelf-life of the urease was also evaluated within 30 days, revealing a high shelf-stability for the as-prepared nanosized artificial urease. Consequentially, the nanosized artificial urease can be practically applied for both urea detection and blood cleaning in the real world.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"Article 110736"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144864722","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":"2025-12-01","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":"Effect of lipopolysaccharide on ganglioside expression in human induced pluripotent stem cell-derived kidney organoids.","authors":"Jae-Sung Ryu, Jin Ok Yu, Ki Kwan Kim, Eun-Jeong Jeong, Min Young Kim, Hyo Gyeong Yun, Eun Bin Song, Ji-Su Kim, Young-Woock Noh, Young-Kug Choo","doi":"10.1016/j.enzmictec.2025.110730","DOIUrl":"10.1016/j.enzmictec.2025.110730","url":null,"abstract":"<p><p>An organoid is a self-organizing, three-dimensional (3D), stem cell-derived structure that closely mimics the structural, cellular, and functional properties of specific organs or tissues. Organoids are widely utilized for assessing drug efficacy, safety, and industrial chemical toxicity. The purpose of this study was to generate a kidney organoid from human induced pluripotent stem cells (iPSCs) and establish a sepsis-associated acute kidney injury (SA-AKI) model by treatment with lipopolysaccharide (LPS). We further analyzed changes in ganglioside expression following LPS treatment in kidney organoids. As a result, we observed that the expression of kidney-specific markers was significantly increased during differentiation. Next, we confirmed that the levels of inflammation-related markers and reactive oxygen species (ROS) were significantly increased, whereas mitochondrial membrane potential (MMPΨ) was significantly reduced in LPS-treated kidney organoids. Interestingly, ganglioside GM3, GM2, GD3, and GD1a expression, as well as their biosynthesis, was notably decreased in LPS-treated kidney organoids. These findings suggest that gangliosides play critical roles in inflammation and may contribute to the pathophysiology of SA-AKI, highlighting the potential of kidney organoids as a valuable model system for studying kidney injury and associated inflammatory responses.</p>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"191 ","pages":"110730"},"PeriodicalIF":3.7,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144816100","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}