Biotechnology Reports最新文献

{"title":"Investigating a new Dillenia ovata endophytic bacteria to produce antioxidants and anti-diabetes activity in vitro and in vivo","authors":"Linh Chi Tran ,&nbsp;Chong Kim Thien Duc ,&nbsp;Tuan Trong Nguyen ,&nbsp;Duy Toan Pham ,&nbsp;Danh Thai Luu ,&nbsp;Trang Thi Xuan Dai","doi":"10.1016/j.btre.2025.e00921","DOIUrl":"10.1016/j.btre.2025.e00921","url":null,"abstract":"<div><div>A novel endophytic bacterium, <em>Bacillus</em> sp. DO-R5, with strong antioxidant and anti-diabetic properties, was isolated from <em>Dillenia ovata</em>, a traditional Vietnamese medicinal plant. <em>Bacillus</em> sp. DO-R5 was identified using morphological characteristics, SEM, and <em>16S rRNA</em> sequencing, demonstrated the highest bioactivity among the 19 isolates. Optimal fermentation conditions (8.9 g/L D-glucose, pH 7.5, 38 °C, and 70.5 h) were determined using the Box-Behnken design. Under these conditions, <em>Bacillus</em> sp. DO-R5 significantly enhanced the production of bioactive compounds including diosmin, rutin, and chlorogenic acid, and exhibited improved <em>in vitro</em> antioxidant, anti-inflammatory, and anti-diabetic activities. <em>In vivo</em>, the extract effectively reduced blood glucose, regulated lipid profiles, supported weight control, and protected organs. These findings emphasize the potential therapeutic use of <em>D. ovata</em> endophytic bacteria as a natural source of anti-diabetic drugs.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00921"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144891941","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enhanced CO2 sequestration and paramylon production in acid-tolerant Euglena gracilis: Growth optimization and metabolic response under varying CO2 concentrations","authors":"Tia Erfianti ,&nbsp;Brilian Ryan Sadewo ,&nbsp;Nugroho Dewayanto ,&nbsp;Adib Fakhruddin Yusuf ,&nbsp;Dedy Kurnianto ,&nbsp;Deviko Mardyansah ,&nbsp;Ikhnu Prawestri Wardani ,&nbsp;Budi Setiadi Daryono ,&nbsp;Eko Agus Suyono ,&nbsp;Marcos ,&nbsp;Arief Budiman","doi":"10.1016/j.btre.2025.e00935","DOIUrl":"10.1016/j.btre.2025.e00935","url":null,"abstract":"<div><div><em>Euglena gracilis</em> is a microalgae suited for acidic environments and efficient CO₂ absorption, making it a strong candidate for biological carbon fixation. This study examined its growth, biomass, lipid and paramylon production, and metabolic responses under varying CO₂ levels (0.04 %, 5 %, 15 %, 30 %). Optimal results were observed at 5 % CO₂, with peak biomass (0.407 ± 0.099 g/L), lipid (0.189 ± 0.025 g/L), and paramylon (0.0159 ± 0.0034 g/L) on day 6. SEM showed oval to ellipsoid paramylon granules (0.5–2.5 µm), while GC–MS revealed isophytol acetate (31.44 %) as the major fatty acid. Upregulation of <em>RubisCO</em> and <em>EgGSL1</em> genes indicated enhanced carbon fixation and paramylon synthesis. A 12 L pilot-scale culture confirmed high CO₂ uptake (0.429 g·L⁻¹·day⁻¹). These findings support <em>E. gracilis</em> as a promising platform for CO₂ sequestration, bioresource production, and paramylon-based bioproducts, with further research needed for industrial scalability.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00935"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145525441","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Numerical modelling and experimental validation of an orifice plate-based hydrodynamic cavitation process for improving the biomass pretreatment","authors":"Shetal Roy ,&nbsp;Souman Rudra ,&nbsp;DI Muhandiram ,&nbsp;MM Roshid","doi":"10.1016/j.btre.2025.e00925","DOIUrl":"10.1016/j.btre.2025.e00925","url":null,"abstract":"<div><div>Hydrodynamic cavitation can be used to pretreat biomass by utilizing the energy released during the collapse of cavitation bubbles. Delignification as pretreatment enhances the biodegradation of lignocellulosic composition. The present study employed a CFD model and experimental validation of the numerical analysis of hydrodynamic cavitation (HC) in multi-hole orifice (MHO) designs under various operating conditions. The total 14 geometry of the orifice plate depends on the plate thickness, the number of holes, and the hole orientation used to analyze and optimize geometry for the biomass pretreatment process. Three phases are used in numerical analysis and experimentation to investigate the effect of particles on cavitation. The simulated results regarding velocity and pressure gradients, turbulence quantities, and vapor volume fractions are critically analyzed and discussed. The cavitation number changes to 0.22 in the experiment and 0.16 in the simulation due to the presence of biomass particles. Orifice plate thickness was found to significantly influence cavitation inception and evolution. 4 mm thickness and nine holes with specific orientations were found to be an optimized geometry with the lowest cavitation number, maximum pressure drop, and highest throat velocity. In the experimentation, 0.8 mm biomass particles were used in the mixture (2 % w/w) to determine the effect of biomass particles on the flow. This result helps identify the critical operating and design parameters and the impact on the cavitation of particles to achieve the desired cavitation phenomena.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00925"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105568","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Improvement of protein quality and reduction of anti-nutritional factors in soybean meal by solid-state fermentation with Bacillus siamensis MH03","authors":"Tanawut Chotinu-kul,&nbsp;Gunjana Theeragool,&nbsp;Duenrut Chonudomkul","doi":"10.1016/j.btre.2025.e00915","DOIUrl":"10.1016/j.btre.2025.e00915","url":null,"abstract":"<div><div>This study investigated the optimal conditions for enhancing protein quality and reducing anti-nutritional factors in soybean meal (SBM) through solid-state fermentation (SSF) with <em>Bacillus.</em> Among 78 isolates, strain MH03 exhibited the highest extracellular enzyme production and efficacy in enhancing SBM quality. Under optimized SSF conditions of 5 kg SBM, 5 cm thickness and 50 % initial moisture for 72 h, strain MH03 increased soluble protein from 3.31±0.21 to 10.16±0.27 g/100 g and significantly reduced anti-nutritional compounds, including glycinin, β-conglycinin, trypsin inhibitor, and oligosaccharides. Crude protein content increased from 47.89±0.07 % to 55.84±0.25 %, with protein solubility increased from 74.96±0.45 % to 90.54±0.28 %, with statistically significant increases. Other nutritional values were also significantly enhanced. Essential amino acids, such as valine, methionine, isoleucine, and lysine also increased. Based on 16S rRNA gene sequencing, MH03 was identified as <em>Bacillus siamensis</em>. These findings highlight the potential of <em>B. siamensis</em> MH03-fermented SBM as a high-quality protein ingredient for animal feed applications.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00915"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144886331","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biodecolorization and Biodegradation of Methyl Orange by Immobilized Pseudomonas aeruginosa Bacterium into SA/PVA Matrix Integrated with MOF UiO-66 Adsorbent","authors":"Sarazen Shalahuddin Akbar,&nbsp;Adi Setyo Purnomo ,&nbsp;Silvia Abdi Pratama,&nbsp;Berlian Imazdalifa,&nbsp;Sifra Thrivelia Krisnia Ayu,&nbsp;Reyza Fadly Maghfiroh,&nbsp;Nur Annisa Kusumawardhani,&nbsp;Ardi Lukman Hakim","doi":"10.1016/j.btre.2025.e00924","DOIUrl":"10.1016/j.btre.2025.e00924","url":null,"abstract":"<div><div>Azo dye, such as methyl orange (MO), is characterized by environmental concerns due to persistence, toxicity, and potential carcinogenic effects. Therefore, this study aimed to investigate the integration of immobilized <em>Pseudomonas aeruginosa</em> (PA) and UiO-66, a zirconium-based metal-organic framework (MOF), into sodium alginate/polyvinyl alcohol (SA/PVA) matrix for biodecolorization and biodegradation of MO dye. Material characterization was carried out by using X-ray diffraction (XRD), Fourier-transform infrared (FTIR), and scanning electron microscopy-energy dispersive X-ray (SEM-EDX) which showed the successful formation of UiO-66 and stable incorporation in SA/PVA/PA beads. The results of adsorption experiments showed that the presence of UiO-66 enhanced MO adsorption capacity by 20.47 % compared to SA/PVA/PA matrix without UiO-66. Kinetic analysis followed the pseudo-second-order model, and adsorption isotherm was best described by the Langmuir model, showing monolayer adsorption behavior. Furthermore, biodecolorization results showed that SA/PVA/UiO-66/PA beads achieved a 92.03 % MO removal rate, indicating a 33.99 % higher than free PA cells. Liquid chromatography–mass spectrometry (LC-MS) analysis confirmed the formation of nine biodegradation products, suggesting successful structural breakdown of MO. These results showed that combining UiO-66 with immobilized PA significantly enhanced both adsorption and biodegradation performance toward MO treatment.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00924"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145048879","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Glycoengineering of plant-produced Pembrolizumab enhances FcRn binding and extends serum half-life in mice","authors":"Christine Joy I. Bulaon ,&nbsp;Janejira Jaratsittisin ,&nbsp;Kaewta Rattanapisit ,&nbsp;Pipob Suwanchaikasem ,&nbsp;Shiying Guo ,&nbsp;Khwanchit Boonha ,&nbsp;Pannamthip Pitaksajjakul ,&nbsp;Nipaporn Simsom ,&nbsp;Vudhiporn Limprasutr ,&nbsp;Waranyoo Phoolcharoen","doi":"10.1016/j.btre.2025.e00927","DOIUrl":"10.1016/j.btre.2025.e00927","url":null,"abstract":"<div><div>Plant systems offer scalable and cost-effective platforms for antibody production, but plant-specific glycans may affect pharmacokinetics and immunogenicity. To evaluate the impact of Fc glycosylation, four Pembrolizumab glycovariants were generated in <em>Nicotiana benthamiana</em>: wild-type glycosylation (Pembro-WT), high-mannose with SEKDEL (Pembro-KD), aglycosylated N297A mutant (Pembro-NG), and a core fucose/xylose-deficient variant (Pembro-XF). Glycoproteins were transiently expressed either in wild-type or ΔXF plants, purified, and characterized for glycan composition, in vitro binding, and in vivo pharmacokinetics. LC-MS confirmed distinct glycoform patterns, while PD-1 binding was retained across all variants. Pembro-XF showed the highest FcRn binding affinity and longest serum half-life (45.83 h) in mice, compared to Pembro-WT (26.7 h), Pembro-KD (32.95 h), Pembro-NG (34.27 h), and Keytruda® (33.26 h). As an initial efficacy evaluation, Pembro-WT demonstrated strong antitumor activity in a murine colon cancer model. These findings support plant glycoengineering as a strategy to enhance antibody pharmacokinetics and advance next generation antibody therapeutics.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00927"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145219779","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery and engineering of bifunctional enzymes for lignocellulose degradation: Metagenomic and computational approaches","authors":"Razieh Goudarzi ,&nbsp;Donya Afshar Jahanshahi ,&nbsp;Arashk Kavousi ,&nbsp;Shohreh Ariaeenejad","doi":"10.1016/j.btre.2025.e00926","DOIUrl":"10.1016/j.btre.2025.e00926","url":null,"abstract":"<div><div>Efficient degradation of lignocellulosic biomass is vital for converting plant-based waste into renewable fuels and chemicals. Owing to its complex composition of cellulose, hemicellulose, and lignin, its enzymatic breakdown often requires multiple enzymes to act synergistically. Bifunctional enzymes that combine two catalytic activities in a single protein offer a promising solution. This review highlights recent advances in the identification and engineering of bifunctional enzymes for lignocellulose degradation, particularly through metagenomics, protein fusion and computational design. Functional pairings, such as cellulase/xylanase, were examined with a focus on their synergistic effects, substrate specificity, and stability. Promiscuous and naturally evolved bifunctional enzymes from extreme or uncultured environments are also discussed. Advances <em>in silico</em> modeling and directed evolution have enhanced enzyme properties such as thermostability and substrate range. The review concludes with an outlook on the challenges and opportunities of implementing bifunctional enzymes to improve the economic and technical viability of biomass conversion.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00926"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145158336","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enhancing enzyme activity of heterologously expressed Chit42 in Nicotiana benthamiana for chitin degradation","authors":"Naser Mirhosseini Motlagh ,&nbsp;Mostafa Motallebi ,&nbsp;Zahra Moghaddassi Jahromi ,&nbsp;Lukhanyo Mekuto","doi":"10.1016/j.btre.2025.e00934","DOIUrl":"10.1016/j.btre.2025.e00934","url":null,"abstract":"<div><div>This study focused on enhancing the activity of the chitinase42 enzyme from <em>Trichoderma atroviride</em>. A Chitin-Binding Domain (ChBD) from <em>T. atroviride</em> chitinase18.10 was incorporated into the genomic DNA of the chitinase42 at the N-terminal using SOEing PCR. The engineered chimeric chitinase42 and the native chitinase42 were cloned into the expression vector pGDDEE, under the control of the synthetic inducible promoter SP-DDEE, resulting in constructs pGDDEENM1 and pGDDEEJN1, respectively. These were introduced into <em>Nicotiana benthamiana</em> using <em>Agrobacterium tumefaciens</em> strain 3101. Enzyme activity was optimized via colorimetric methods. Findings revealed optimal transient expression conditions: expression induction by spraying methyl jasmonate and sampling five days post- induction (5 DPI). The chimeric chitinase42 exhibited its highest enzymatic activity, surpassing chitinase42, at 40 °C and pH 4 with 1.55-fold higher than the native chitinase42 (lacking ChBD). Crucially, the chimeric chitinase42 demonstrated superior activity to the native enzyme, underscoring the potential for enhanced chitin degradation.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00934"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145362598","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Solving the light chain mismatch of IgG-like bispecific antibody by utilizing 2A peptide based FaBody platform","authors":"Dong Li ,&nbsp;Pengfan Zheng ,&nbsp;Xuejing Yao ,&nbsp;Baopeng Zhang ,&nbsp;Jiekun Zhang ,&nbsp;Yaocheng Qu ,&nbsp;Shasha Yun ,&nbsp;Yanzhen Li ,&nbsp;Shanshan Chen ,&nbsp;Jianmin Fang","doi":"10.1016/j.btre.2025.e00917","DOIUrl":"10.1016/j.btre.2025.e00917","url":null,"abstract":"<div><div>Bispecific antibodies (BsAbs), engineered to target multiple antigens or epitopes simultaneously, promise enhanced therapeutic efficacy over traditional monoclonal antibodies (mAbs). However, the complex BsAbs structure presents significant production challenges, particularly chain mismatch issues. This study presents a novel approach utilizing 2A peptides within a FaBody platform to address light chain mismatches in IgG-like BsAbs. By leveraging self-cleaving 2A peptides, stable expression in mammalian cells significantly improves the accuracy of antibody chain assembly. This strategy markedly enhances the production of correctly assembled IgG-like BsAbs, providing a promising solution to critical challenges in BsAbs drug development.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00917"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105569","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Sargassum incisifolium and Ulva spp metabolites activity and their molecular dynamics simulation against Fusarium oxysporum 14-alpha-demethylase","authors":"Omolola Aina ,&nbsp;Adewale O. Fadaka ,&nbsp;Daniel Watson ,&nbsp;Cecilia Y. Ojemaye ,&nbsp;Denzil R. Beukes ,&nbsp;Kudakwashe Nyambo ,&nbsp;Kudzanai Tapfuma ,&nbsp;Vuyo Mavumengwana ,&nbsp;Nicole R. S Sibuyi ,&nbsp;Marshall Keyster ,&nbsp;Ashwil Klein","doi":"10.1016/j.btre.2025.e00919","DOIUrl":"10.1016/j.btre.2025.e00919","url":null,"abstract":"<div><div>Fusarium oxysporum, a major agricultural pathogen, poses severe risks to crops worldwide. With increasing resistance to conventional antifungal agents, there is an urgent need for alternative treatments. Seaweeds such as <em>Ulva spp.</em> and Sargassum incisifolium are promising sources of bioactive compounds that may offer novel antifungal properties. This study investigates the antifungal activity of acetone extracts from <em>Ulva spp.</em> and Sargassum incisifolium against <em>F. oxysporum</em>, with the goal of identifying specific bioactive compounds responsible for this activity and evaluating their effectiveness quantitatively. We prepared acetone extracts from both seaweed species and assessed their antifungal activity using a series of in vitro assays. The total phenolic content (TPC) and antioxidant capacity were determined for each extract. LC-qTOF-MS/MS was employed for phytochemical profiling, while molecular docking and molecular dynamics simulations were used to predict interactions between identified compounds and the 14-alpha-demethylase enzyme of <em>F. oxysporum</em>. The TPC was 2.72±0.009 and 2.23±0.009 GAE/mg dry weight for <em>Ulva spp</em> and <em>S. incisifolium</em>. Additionally, significant antioxidant activity was observed, with IC50 values of 8.38±0.06 µg/mL for <em>Ulva spp</em> and 8.01±0.07 µg/mL for <em>S. incisifolium</em>, which are comparable to ascorbic acid (5.23±0.04 µg/mL). Phytochemical analysis revealed high levels of terpenoids, phenolics, and fatty acids. In molecular docking, compounds such as medicocarpin, corynanthine, and merulinic acid demonstrated strong binding affinities (binding energies ≤ -7.5 kcal/mol). Molecular dynamics simulations confirmed stable interactions over 100 ns, with medicocarpin exhibiting the most stable binding profile. The study demonstrates that acetone extracts of <em>Ulva spp.</em> and <em>S. incisifolium</em> possess significant antifungal activity against <em>F. oxysporum</em>. Medicocarpin, in particular, emerged as a promising candidate for further development as an antifungal agent. These findings underscore the potential of seaweed-derived compounds as antifungal agents against fungal pathogens and highlight the need for further investigation into their practical applications in plant disease management. Specifically, Medicocarpin emerged as a promising <em>in silico</em> candidate, warranting further experimental validation.</div></div>","PeriodicalId":38117,"journal":{"name":"Biotechnology Reports","volume":"48 ","pages":"Article e00919"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144996615","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}