Journal of biotechnology最新文献

{"title":"Comparative characterisation of autotrophic and heterotrophic isopropanol formation by Cupriavidus necator in shake flasks","authors":"I. Weickardt ,&nbsp;E. Lombard ,&nbsp;A. Zhang ,&nbsp;L. Blank ,&nbsp;S.E. Guillouet","doi":"10.1016/j.jbiotec.2025.03.011","DOIUrl":"10.1016/j.jbiotec.2025.03.011","url":null,"abstract":"<div><div>Autotrophic cultivation offers a path to carbon-neutral bioproduction, which is increasingly valuable in the context of climate change mitigation. In this study, the production of isopropanol by <em>Cupriavidus necator</em> is used as an example for CO₂ valorisation, and a simple shake bottle system is introduced to facilitate the development of aerobic autotrophic cultivation processes and strain screening. Applying 1.5 bar overpressure in the bottle's headspace enhances gas transfer while pressure decrease was shown to be correlated to biomass and product formation, allowing to follow metabolic activity without sampling. After optimizing cultivation parameters and nickel feeding strategy, the system was applied to compare three different isopropanol-producing strains. The highest autotrophically obtained isopropanol concentration was 2.2 ± 0.5 g L⁻¹ with a specific yield of 0.9 ± 0.2 g g_CDW⁻¹ and a minimal by-product concentration of 0.05 ± 0.01 g L⁻¹ acetone. Heterotrophic cultivations were carried out for comparison, obtaining up to 3.4 ± 0.2 g L⁻¹ final isopropanol concentration with a specific yield of 1.4 ± 0.1 g g_CDW⁻¹. Although the use of CO₂ instead of fructose resulted in a slower process, the overall isopropanol production is promising. This study provides valuable insights into strain behaviour while demonstrating the utility of the presented shake bottle system for advancing autotrophic process development.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"403 ","pages":"Pages 1-8"},"PeriodicalIF":4.1,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143691831","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ethanolysis of degummed soybean oil using magnetic CLEAs from Eversa® Transform","authors":"Letícia Passos Miranda ,&nbsp;José Renato Guimarães ,&nbsp;Roberto Fernandez-Lafuente ,&nbsp;Paulo Waldir Tardioli","doi":"10.1016/j.jbiotec.2025.03.010","DOIUrl":"10.1016/j.jbiotec.2025.03.010","url":null,"abstract":"<div><div>Eversa^@ Transform magnetic crosslinked enzyme aggregates (Eversa-mCLEA) have been used to produce fatty acid ethyl esters (FAEEs) through the ethanolysis of soybean oil. Some variables influencing this reaction were studied using an experimental statistical design. After 12 hours of reaction, a maximum FAEEs yield of 64 wt% was obtained using 4 U_est/g oil of Eversa-mCLEA, an anhydrous ethanol/refined oil molar ratio of 11, and a temperature of 40°C. Degummed oil and hydrated ethanol were used as more cost-effective alternatives, leading to an increase in FAEEs yield (up to 73 wt%). The initial reaction rate increased with a lower molar ratio of hydrated ethanol/degummed oil; however, the final yield remained similar. The combined use of Eversa-mCLEA and Lipozyme 435 resulted in 86 wt% FAEEs and 4 wt% of free fatty acids (FFAs) after 24 hours. A caustic polishing step of the product yielded 90 wt% FAEEs and 0.17 wt% FFAs. These findings show that, using these substrates, a more effective purification step (such as fractional distillation) is required for the product to meet international standards for biodiesel commercialization.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 79-86"},"PeriodicalIF":4.1,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143687925","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An efficient lysate-based approach for biosynthesis of the pyrrolobenzodiazepine natural product tilimycin","authors":"Monica R. MacDonald ,&nbsp;Andrew M. Gulick","doi":"10.1016/j.jbiotec.2025.03.012","DOIUrl":"10.1016/j.jbiotec.2025.03.012","url":null,"abstract":"<div><div>Many bacteria use nonribosomal peptide synthetases (NRPSs), a family of multidomain enzymes that produce peptide natural products using an assembly line strategy. One class of such compounds are pyrrolobenzodiazepines, which have DNA alkylating activity. One example is tilimycin, a compound produced by the human gut microbiota that plays a role in epithelial damage during antibiotic-associated dysbiosis. The production of analogs of these natural products may facilitate the discovery of novel bioactive molecules. However, the synthesis of these natural products typically requires significant resources and time to produce in sufficient amounts for microbial and biochemical testing. Biocatalysis offers an environmentally friendly approach, but enzyme yield and stability, particularly with large multidomain enzymes that are often used in natural product pathways, can limit biochemical reactions with purified protein. Here, we demonstrate a cell lysate-based method to synthesize the nonribosomal peptide natural product tilimycin directly from the substrates 3-hydroxyanthranilic acid and L-proline with lysates from <em>E. coli</em> cell lines that express the tilimycin biosynthetic proteins. We present our protocol optimization and scale-up to produce tilimycin in a fast, efficient manner.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 87-95"},"PeriodicalIF":4.1,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143687924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synergistic interaction of AaMYC2 and AaMYC2-LIKE enhances artemisinin production in Artemisia annua L.","authors":"Ishfaq Majid Hurrah ,&nbsp;Mohammad ,&nbsp;Amit Kumar ,&nbsp;Nazia Abbas","doi":"10.1016/j.jbiotec.2025.03.007","DOIUrl":"10.1016/j.jbiotec.2025.03.007","url":null,"abstract":"<div><div>Artemisinin-based combination therapies recommended by WHO marks <em>Artemisia annua</em> as the only natural source of artemisinin fighting deadly disease, Malaria. In this study, we isolated two transcription factors, AaMYC2 and AaMYC2-LIKE, from <em>A. annua</em> and investigated their role in regulating artemisinin biosynthetic pathway. Our findings depict that both AaMYC2 and AaMYC2-LIKE are transcriptionally active and, when co-transformed in yeast cells, significantly enhance β-galactosidase activity in transactivation assays as compared to their individual transformations. Furthermore, Yeast two-hybrid (Y2H) and Biomolecular fluorescence complementation assays revealed AaMYC2 physically interacts with AaMYC2-LIKE in yeast cells and in the nucleus of onion epidermal cells respectively. Generation of transient transgenic over expression and co-expression lines of AaMYC2 and AaMYC2-LIKE resulted in elevated expression of artemisinin biosynthetic genes and trichome development genes in co-expression lines as compared to individual transgenic lines and wildtype. Importantly, the glandular trichome density and artemisinin content was also significantly higher in co-transformed transgenic lines compared to individual AaMYC2 and AMYC2-LIKE transgenic lines. Conversely, artemisinin content was markedly reduced in AaMYC2-RNAi lines, underscoring the critical role of functional AaMYC2 in synergistic regulation with AaMYC2-LIKE. Altogether the above studies provide valuable insights into the regulatory networks of MYC type bHLH transcription factors in controlling economically and medically important pathway in <em>A. annua.</em></div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 69-78"},"PeriodicalIF":4.1,"publicationDate":"2025-03-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143663424","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeted inhibition of oral biofilm formation using phage-derived high-affinity peptides","authors":"Jaewoong Lee ,&nbsp;Woo-Ri Shin ,&nbsp;Yang-Hoon Kim ,&nbsp;Ji-Young Ahn ,&nbsp;Soryong Chae ,&nbsp;Jiho Min","doi":"10.1016/j.jbiotec.2025.03.009","DOIUrl":"10.1016/j.jbiotec.2025.03.009","url":null,"abstract":"<div><div>Dental caries, commonly known as tooth decay, poses a significant oral health challenge affecting individuals of all age groups. While dietary factors play a role, tooth decay primarily results from the activity of various oral bacteria that form biofilms in the oral cavity. In this study, we employed the phage display technique to identify high-affinity peptides capable of binding specifically to three oral bacteria strains: <em>Streptococcus mutans</em>, <em>Streptococcus oralis</em>, <em>and Lactobacillus casei</em>. Four selected peptides underwent binding affinity testing for each target bacterium, revealing that three of them exhibited specific binding capabilities, effectively inhibiting biofilm formation. This study demonstrates the efficacy of engineered phages in identifying high-affinity peptides that selectively target oral bacteria. These peptides hold promise for preventing oral biofilm formation, a significant contributor to oral diseases and dental caries. This innovative approach opens doors to novel therapeutic strategies for addressing oral health issues. The findings may spur further research into the utilization of phages and peptides as potential anti-biofilm agents, potentially revolutionizing the field of oral health.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 51-58"},"PeriodicalIF":4.1,"publicationDate":"2025-03-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143648586","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Laboratory evolution and characterization of nitrate-resistant phosphite dehydrogenase (PtxD) for enhanced cyanobacterial cultivation","authors":"Gamal Nasser Abdel-Hady ,&nbsp;Tomohito Hino ,&nbsp;Hiroki Murakami ,&nbsp;Akari Miwa ,&nbsp;Linh Thi Thuy Cao ,&nbsp;Tomomi Kuroki ,&nbsp;Kaori Nimura-Matsune ,&nbsp;Takeshi Ikeda ,&nbsp;Takenori Ishida ,&nbsp;Hisakage Funabashi ,&nbsp;Satoru Watanabe ,&nbsp;Akio Kuroda ,&nbsp;Ryuichi Hirota","doi":"10.1016/j.jbiotec.2025.03.008","DOIUrl":"10.1016/j.jbiotec.2025.03.008","url":null,"abstract":"<div><div>Phosphite dehydrogenase (PtxD) catalyzes NAD⁺-dependent oxidation of phosphite (Pt) to phosphate (Pi), offering various biotechnological applications, such as the creation of Pt-dependency for the biological containment of genetically modified organisms. Previously, we established a Pt-dependent cyanobacterial strain (RH714) by expressing PtxD and a reduced phosphorous compound-specific transporter (HtxBCDE) in <em>Synechococcus elongatus</em> PCC 7942 devoid of its endogenous Pi transporters. This strain demonstrated strict Pt dependency but failed to grow in unbuffered BG-11 medium supplemented with 2 % CO₂ owing to medium acidification below approximately pH 6.5. The present study aimed to overcome this limitation by passaging the RH714 strain in an unbuffered growth medium, resulting in mutants capable of growing without buffering. The mutant strains carried a Gly157Ser mutation in the Rossmann fold domain of PtxD, leading to approximately five- and eight-fold higher <em>K</em>_m values for NAD⁺ and Pt, respectively, compared with the wild-type enzyme. Interestingly, PtxD^G157S exhibited enhanced resistance to nitrate, a major component of BG-11, suggesting that reduced substrate affinity mitigates nitrate inhibition at lower pH levels. Further kinetic analysis revealed that nitrate inhibits wild-type PtxD through an uncompetitive mechanism, targeting the enzyme-substrate complex at an allosteric site. Consequently, the PtxD^G157S mutation reduces nitrate binding, facilitating sustained growth of Pt-dependent strains under conditions without pH buffering. These findings imply that PtxD^G157S could significantly enhance the applicability of Pt-dependent cyanobacterial strain.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 59-68"},"PeriodicalIF":4.1,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143630498","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Strengthening core-region hydrogen-bond networks and rigidifying surface loop to enhance thermostability of an (R)-selective transaminase converting chiral hydroxyl amines","authors":"Yuwen Wei ,&nbsp;Fulong Li ,&nbsp;Yukun Zheng ,&nbsp;Youxiang Liang ,&nbsp;Yan Du ,&nbsp;Huimin Yu","doi":"10.1016/j.jbiotec.2025.03.006","DOIUrl":"10.1016/j.jbiotec.2025.03.006","url":null,"abstract":"<div><div>Transaminases have important applications in the synthesis of drug intermediates such as chiral amines. However, natural transaminases exhibit suboptimal thermal stability, limiting their further applications. Building upon an <em>Rhodobacter sp.</em>-derived (<em>R</em>)-selective transaminase (<em>Rb</em>TA), we report a dual-region coupling engineering approach to improve thermostability of <em>Rb</em>TA by strengthening the core hydrogen-bond networks and rigidifying the flexible surface loop. Through single strategy, we identified 4 thermostability improved single mutations, among which I249Q demonstrated the most substantial improvement, achieving a 18-fold increase in half-life (<span><math><msubsup><mrow><mi>t</mi></mrow><mrow><mn>1</mn><mo>/</mo><mn>2</mn></mrow><mrow><mn>40</mn></mrow></msubsup></math></span>) and a 11.2 ℃ increase in <span><math><msubsup><mrow><mi>T</mi></mrow><mrow><mn>50</mn></mrow><mrow><mn>10</mn></mrow></msubsup></math></span>. Then in strategic coupling, the synergistic effect of dual-region modification was observed in both thermal stability and activity enhancement, as mutant with the best high-temperature catalytic performance, R136P/F228Y, had its <span><math><msubsup><mrow><mi>T</mi></mrow><mrow><mn>50</mn></mrow><mrow><mn>10</mn></mrow></msubsup></math></span> improved by 7.1℃ and exhibited a 4.2-fold increase in <em>k</em>_cat/<em>K</em>_m towards (<em>R</em>)-3-amino-1-butanol. Finally, R136P/F228Y achieved a 20.5 % improvement in conversion over WT in an analytical-scale synthesis in 72 h at a 5 ℃ elevated catalytic temperature. Molecular dynamics simulations demonstrated that the synergy of the formation of new hydrogen bonds and decrease in flexibility accounted for the thermostability improvements. This study provides guidance for enhancing thermostability of similar fold-type enzymes without impairing enzymatic activity in an efficient manner.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 39-50"},"PeriodicalIF":4.1,"publicationDate":"2025-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143585843","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Establishment of high-efficiency hairy root and genetic transformation system in Cynanchum stauntonii","authors":"Jingyi Zhang ,&nbsp;Xingfang Mao ,&nbsp;Bisheng Huang ,&nbsp;Mi Lei ,&nbsp;Yuhuan Miao ,&nbsp;Dahui Liu","doi":"10.1016/j.jbiotec.2025.02.006","DOIUrl":"10.1016/j.jbiotec.2025.02.006","url":null,"abstract":"<div><div><em>Cynanchum stauntonii</em> is an important medicinal plant with antitussive effect, and its roots and rhizomes are the main medicinal part. The saponins of <em>C. stauntonii</em> are generally considered to be the active ingredients. The hairy root (HR) system is an important production system for secondary metabolites. However, the systems for HR induction and transformation of <em>C. stauntonii</em> have not been reported. Using <em>Agrobacterium rhizogenes</em> A4 and 20-day young stems, we induced HRs in <em>C. stauntonii</em> with a 79.5 % success rate. The results showed that the content of steroid alkaloids, such as cortisone, tomatidine, jurubine and 18-hydroxycorticosterone in HRs, were increased compared with normal roots (NRs). We applied three elicitors—chitosan, turpentine, and MeJA to enhance the biosynthesis of active components in HRs. The results showed that 10 mg/L chitosan could increase the content of active ingredients in HRs by over two-fold. Additionally, we successfully established a genetic hairy root transformation system with a 56.36 % success rate, enabling betalain production up to 1.24 mg/g in dry weight of HRs. This research is the first to report HR induction and transformation systems for <em>C. stauntonii</em>, laying a crucial foundation for future functional genomics studies and the production of active components in this valuable medicinal plant.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 21-29"},"PeriodicalIF":4.1,"publicationDate":"2025-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143597014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bioproducts from renewable methanol: The paraformaldehyde approach","authors":"Jan A.M. de Bont ,&nbsp;Bram J. Visscher ,&nbsp;Timo J.P. van Roosmalen ,&nbsp;Jan Wery ,&nbsp;Bart W. Swinkels ,&nbsp;Ger G. Bemer","doi":"10.1016/j.jbiotec.2025.03.004","DOIUrl":"10.1016/j.jbiotec.2025.03.004","url":null,"abstract":"<div><div>Green methanol as feedstock in biotech operations at large scales is receiving in-depth attention for the production of Single Cell Protein (SCP) and circular chemicals. Several decades ago, cheap fossil-derived methanol was seen as an attractive feedstock. Now, renewable rather than fossil-derived methanol is in focus since its utilization does not depend on fossil resources and importantly it does not compete with food sources. Despite decade-long efforts, the biotech approaches have not been successful in generating economically viable large-scale production based on methanol. This impressive negative track record is to be attributed to the relatively reduced chemical nature of methanol, which implies excessive oxygen demands during fermentations. Hence, for large-scale methanol fermentations, it is essential to minimize oxygen budgets to arrive at economically-viable production processes. In this short communication, a new approach is described in reducing the oxygen footprint by employing the less-reduced compound paraformaldehyde which, via standard procedures, can be obtained chemically from methanol. It is a water-insoluble polymer, which slowly releases formaldehyde at ambient temperatures depending on either pH or temperature. Three methylotrophic microbes were demonstrated to metabolize formaldehyde as chemically released from the non-toxic paraformaldehyde. <em>Methylophilus methylotrophus</em> kept the monomeric formaldehyde below the detection limit in a stirred-tank bioreactor during a 20-hour run on paraformaldehyde. Based on the current work, it is concluded that paraformaldehyde is a highly-suitable feedstock for producing either SCP or numerous circular chemicals as derived from renewable methanol.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 1-4"},"PeriodicalIF":4.1,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143585842","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The promoter of Zymomonas mobilis respiratory NADH dehydrogenase (ndh) is induced by oxygen","authors":"Marta Rubina ,&nbsp;Inese Strazdina ,&nbsp;Reinis Rutkis,&nbsp;Uldis Kalnenieks","doi":"10.1016/j.jbiotec.2025.03.005","DOIUrl":"10.1016/j.jbiotec.2025.03.005","url":null,"abstract":"<div><div>Expression of the genes of engineered green fluorescent protein and the <em>Zymomonas mobilis</em> native malic enzyme from plasmid vectors under the <em>Z. mobilis</em> respiratory NADH dehydrogenase promoter (Pndh) was strongly enhanced by aeration, both in the wild type Zm6 and its respiratory-deficient mutant derivative Zm6-<em>ndh</em> backgrounds. Pndh in aerobically growing cultures was activated by about an order of magnitude relative to non-aerated control. Its induction approached the maximum level already at moderate aeration (1–5 % oxygen saturation in the medium). The strength of Pndh under aerobic conditions was comparable to, or even surpassed that of the strong <em>Z. mobilis</em> native promoter of glyceraldehyde-3-phosphate dehydrogenase. Although the mechanism of its oxygen-dependent induction is not known, Pndh might serve as a versatile inducible promoter for <em>Z. mobilis</em> metabolic engineering.</div></div>","PeriodicalId":15153,"journal":{"name":"Journal of biotechnology","volume":"402 ","pages":"Pages 5-8"},"PeriodicalIF":4.1,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143585844","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}