Engineering MicrobiologyPub Date : 2024-09-01Epub Date: 2024-07-22DOI: 10.1016/j.engmic.2024.100163
I. C. Cunha-Ferreira , C. S. Vizzotto , T. D. Frederico , J. Peixoto , L. S Carvalho , M. R. Tótola , R. H. Krüger
{"title":"Impact of Paenibacillus elgii supernatant on screening bacterial strains with potential for biotechnological applications","authors":"I. C. Cunha-Ferreira , C. S. Vizzotto , T. D. Frederico , J. Peixoto , L. S Carvalho , M. R. Tótola , R. H. Krüger","doi":"10.1016/j.engmic.2024.100163","DOIUrl":"10.1016/j.engmic.2024.100163","url":null,"abstract":"<div><p>The biotechnological industry faces a crucial demand for novel bioactive compounds, particularly antimicrobial agents, to address the rising challenge of bacterial resistance to current available antibiotics. Traditional strategies for cultivating naturally occurring microorganisms often limit the discovery of novel antimicrobial producers. This study presents a protocol for targeted selection of bacterial strains using the supernatant of <em>Paenibacillus elgii</em>, which produces abundant signal molecules and antimicrobial peptides. Soil samples were inoculated in these enriched culture media to selectively cultivate bacteria resistant to the supernatant, indicating their potential to produce similar compounds. The bacterial strains isolated through this method were assessed for their antibacterial activity. In addition, the functional annotation of the genome of one of these strains revealed several gene clusters of biotechnological interest. This study highlights the effectiveness of using this approach for selective cultivation of microorganisms with potential for biotechnological applications.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 3","pages":"Article 100163"},"PeriodicalIF":0.0,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000250/pdfft?md5=3320eb58e754f7bdc2a2f5525731fd2b&pid=1-s2.0-S2667370324000250-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141846527","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Engineering MicrobiologyPub Date : 2024-09-01Epub Date: 2024-06-25DOI: 10.1016/j.engmic.2024.100162
Maofeng Wang , Cancan Wu , Nan Liu , Xiaoqiong Jiang , Hongjie Dong , Shubao Zhao , Chaonan Li , Sujuan Xu , Lichuan Gu
{"title":"Regulation of protein thermal stability and its potential application in the development of thermo-attenuated vaccines","authors":"Maofeng Wang , Cancan Wu , Nan Liu , Xiaoqiong Jiang , Hongjie Dong , Shubao Zhao , Chaonan Li , Sujuan Xu , Lichuan Gu","doi":"10.1016/j.engmic.2024.100162","DOIUrl":"10.1016/j.engmic.2024.100162","url":null,"abstract":"<div><p>The coronavirus disease 2019 (COVID-19) pandemic has highlighted the importance of developing novel vaccines. An ideal vaccine should trigger an intense immune reaction without causing significant side effects. In this study we found that substitution of tryptophan located in the cores of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) protein structures with certain smaller amino acids resulted in variants with melting temperatures of 33–37 °C. An enzyme activity assay indicated that the proteolytic activity of the main proteinase (3CL<sup>pro</sup>) decreased sharply when the environmental temperature exceeded the melting temperature, implying that other protein variants may lose most of their functions under the same conditions. This finding suggests that a virus variant containing engineered proteins with melting temperatures of 33–37 °C may only be functional in the upper respiratory tract where the temperature is about 33 °C, but will be unable to invade internal organs, which maintain temperatures above 37 °C, thus making it possible to construct temperature-sensitive attenuated vaccines.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 3","pages":"Article 100162"},"PeriodicalIF":0.0,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000249/pdfft?md5=678b37931cc38b0eac77aed4ffe7562b&pid=1-s2.0-S2667370324000249-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141961076","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Engineering MicrobiologyPub Date : 2024-09-01Epub Date: 2024-06-03DOI: 10.1016/j.engmic.2024.100155
Wei-feng Hu, Yan Wang, Xiao-ran Yue, Wei-wei Xue, Wei Hu, Xin-jing Yue, Yue-Zhong Li
{"title":"An upgraded Myxococcus xanthus chassis with enhanced growth characteristics for efficient genetic manipulation","authors":"Wei-feng Hu, Yan Wang, Xiao-ran Yue, Wei-wei Xue, Wei Hu, Xin-jing Yue, Yue-Zhong Li","doi":"10.1016/j.engmic.2024.100155","DOIUrl":"10.1016/j.engmic.2024.100155","url":null,"abstract":"<div><p>Myxobacteria are well known for multicellular social behaviors and valued for biosynthesis of natural products. Myxobacteria social behaviors such as clumping growth severely hamper strain cultivation and genetic manipulation. Using <em>Myxococcus xanthus</em> DK1622, we engineered Hu04, which is deficient in multicellular behavior and pigmentation. Hu04, while maintaining nutritional growth and a similar metabolic background, exhibits improved dispersed growth, streamlining operational procedures. It achieves high cell densities in culture and is promising for synthetic biology applications.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 3","pages":"Article 100155"},"PeriodicalIF":0.0,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000183/pdfft?md5=c2064724dd08cca2123f11fd56275bb0&pid=1-s2.0-S2667370324000183-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141279154","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Engineering MicrobiologyPub Date : 2024-09-01Epub Date: 2024-06-04DOI: 10.1016/j.engmic.2024.100156
Senfeng Zhang , Shengsheng Ma , Feizuo Wang , Chunyi Hu
{"title":"Dual role of phage terminase in Salmonella enterica oxidative stress response","authors":"Senfeng Zhang , Shengsheng Ma , Feizuo Wang , Chunyi Hu","doi":"10.1016/j.engmic.2024.100156","DOIUrl":"10.1016/j.engmic.2024.100156","url":null,"abstract":"<div><p>The adaptive survival mechanisms of bacterial pathogens under host-induced stress are crucial for understanding pathogenesis. Recently, Uppalapati et al. revealed a unique dual function of the Gifsy-1 prophage terminase in <em>Salmonella enterica</em>: it acts as a transfer ribonuclease (tRNase) under oxidative stress. The Gifsy-1 prophage terminase targets and fragments tRNA<sup>Leu</sup> to halt translation and temporarily impairs bacterial growth when exposed to high levels of ROS generated by the host immune cells. This response not only preserves genomic integrity by facilitating DNA repair but also inhibits prophage mobilization, thereby aiding in bacterial survival within vertebrate hosts. This study highlights a novel intersection between phage biology and bacterial adaptive strategies.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 3","pages":"Article 100156"},"PeriodicalIF":0.0,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000158/pdfft?md5=b9a7cbe69de92bd35790678ac162c682&pid=1-s2.0-S2667370324000158-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141275040","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Engineering MicrobiologyPub Date : 2024-09-01Epub Date: 2024-08-03DOI: 10.1016/j.engmic.2024.100164
Ruken Sariboga , Omer Faruk Sarioglu
{"title":"Cellulolytic characterization of the rumen-isolated Acinetobacter pittii ROBY and design of a potential controlled-release drug delivery system","authors":"Ruken Sariboga , Omer Faruk Sarioglu","doi":"10.1016/j.engmic.2024.100164","DOIUrl":"10.1016/j.engmic.2024.100164","url":null,"abstract":"<div><p>A novel cellulolytic bacterial strain, ROBY, was isolated from a bovine rumen sample using the enrichment culture method. This isolate was found to be <em>Acinetobacter pittii</em>, with >99 % similarity according to 16S rRNA gene sequence analysis. The potential use of this strain in combination with doxorubicin (Dox)-integrated cellulose nanoparticles (Dox-CNPs) was evaluated as a proof-of-concept study for the further development of this approach as a novel controlled-release drug delivery strategy. The isolate can utilize CNPs as the sole carbon source for growth and degrade both Dox-CNPs and empty CNPs with high efficiency. Extracellular cellulases isolated from bacteria may also be used to trigger Dox release. The results also demonstrated that the release of Dox into the environment due to nanoparticle degradation in the samples incubated with Dox-CNPs significantly affected bacterial cell viability (∼75 % decrease), proving the release of Dox due to bacterial cellulase activity and suggesting the great potential of this approach for further development.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 3","pages":"Article 100164"},"PeriodicalIF":0.0,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000262/pdfft?md5=154741f24ca8241e1873123c2ea33593&pid=1-s2.0-S2667370324000262-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141963284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Engineering MicrobiologyPub Date : 2024-09-01Epub Date: 2024-08-17DOI: 10.1016/j.engmic.2024.100165
Wenya Su , Wenjia Wang , Ling Li , Mengge Zhang , Hai Xu , Chengzhang Fu , Xiuhua Pang , Mingyu Wang
{"title":"Mechanisms of tigecycline resistance in Gram-negative bacteria: A narrative review","authors":"Wenya Su , Wenjia Wang , Ling Li , Mengge Zhang , Hai Xu , Chengzhang Fu , Xiuhua Pang , Mingyu Wang","doi":"10.1016/j.engmic.2024.100165","DOIUrl":"10.1016/j.engmic.2024.100165","url":null,"abstract":"<div><p>Tigecycline serves as a critical “final-resort” antibiotic for treating bacterial infections caused by multidrug-resistant bacteria for which treatment options are severely limited. The increasing prevalence of tigecycline resistance, particularly among Gram-negative bacteria, is a major concern. Various mechanisms have been identified as contributors to tigecycline resistance, including upregulation of nonspecific Resistance Nodulation Division (RND) efflux pumps due to mutations in transcriptional regulators, enzymatic modification of tigecycline by monooxygenase enzymes, and mutations affecting tigecycline binding sites. This review aims to consolidate our understanding of tigecycline resistance mechanisms in Gram-negative bacteria and offer insights and perspectives for further drug development.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 3","pages":"Article 100165"},"PeriodicalIF":0.0,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000274/pdfft?md5=2ad09fce1eeff0ac4a7f1759375e712e&pid=1-s2.0-S2667370324000274-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142075847","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Engineering MicrobiologyPub Date : 2024-09-01Epub Date: 2024-02-17DOI: 10.1016/j.engmic.2024.100141
Ting Cai , Xinyu Gao , Xiaoyan Qi , Xiaolei Wang , Ruijun Liu , Lei Zhang , Xia Wang
{"title":"Role of the cathode chamber in microbial electrosynthesis: A comprehensive review of key factors","authors":"Ting Cai , Xinyu Gao , Xiaoyan Qi , Xiaolei Wang , Ruijun Liu , Lei Zhang , Xia Wang","doi":"10.1016/j.engmic.2024.100141","DOIUrl":"10.1016/j.engmic.2024.100141","url":null,"abstract":"<div><p>The consumption of non-renewable fossil fuels has directly contributed to a dramatic rise in global carbon dioxide (CO<sub>2</sub>) emissions, posing an ongoing threat to the ecological security of the Earth. Microbial electrosynthesis (MES) is an innovative energy regeneration strategy that offers a gentle and efficient approach to converting CO<sub>2</sub> into high-value products. The cathode chamber is a vital component of an MES system and its internal factors play crucial roles in improving the performance of the MES system. Therefore, this review aimed to provide a detailed analysis of the key factors related to the cathode chamber in the MES system. The topics covered include inward extracellular electron transfer pathways, cathode materials, applied cathode potentials, catholyte pH, and reactor configuration. In addition, this review analyzes and discusses the challenges and promising avenues for improving the conversion of CO<sub>2</sub> into high-value products via MES.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 3","pages":"Article 100141"},"PeriodicalIF":0.0,"publicationDate":"2024-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000043/pdfft?md5=0045968362299ca70bded635c93f6f6d&pid=1-s2.0-S2667370324000043-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139966064","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Engineering MicrobiologyPub Date : 2024-06-01Epub Date: 2024-03-26DOI: 10.1016/j.engmic.2024.100148
Xiaoyan Qi , Huangwei Cai , Xiaolei Wang , Ruijun Liu , Ting Cai , Sen Wang , Xueying Liu , Xia Wang
{"title":"Electricity generation by Pseudomonas putida B6-2 in microbial fuel cells using carboxylates and carbohydrate as substrates","authors":"Xiaoyan Qi , Huangwei Cai , Xiaolei Wang , Ruijun Liu , Ting Cai , Sen Wang , Xueying Liu , Xia Wang","doi":"10.1016/j.engmic.2024.100148","DOIUrl":"10.1016/j.engmic.2024.100148","url":null,"abstract":"<div><p>Microbial fuel cells (MFCs) employing <em>Pseudomonas putida</em> B6-2 (ATCC BAA-2545) as an exoelectrogen have been developed to harness energy from various conventional substrates, such as acetate, lactate, glucose, and fructose. Owing to its metabolic versatility, <em>P. putida</em> B6-2 demonstrates adaptable growth rates on diverse, cost-effective carbon sources within MFCs, exhibiting distinct energy production characteristics. Notably, the anode chamber's pH rises with carboxylates' (acetate and lactate) consumption and decreases with carbohydrates' (glucose and fructose) utilization. The MFC utilizing fructose as a substrate achieved the highest power density at 411 mW m<sup>−2</sup>. Initial analysis revealed that <em>P. putida</em> B6-2 forms biofilms covered with nanowires, contributing to bioelectricity generation. These microbial nanowires are likely key players in direct extracellular electron transport through physical contact. This study established a robust foundation for producing valuable compounds and bioenergy from common substrates in bioelectrochemical systems (BESs) utilizing <em>P. putida</em> as an exoelectrogen.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 2","pages":"Article 100148"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000110/pdfft?md5=eff030301bd91a1d0c97ae88c88b75b9&pid=1-s2.0-S2667370324000110-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140399510","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Engineering MicrobiologyPub Date : 2024-06-01Epub Date: 2023-09-09DOI: 10.1016/j.engmic.2023.100108
Xianni Qi , Zhen Wang , Yuping Lin , Yufeng Guo , Zongjie Dai , Qinhong Wang
{"title":"Elucidation and engineering mitochondrial respiratory-related genes for improving bioethanol production at high temperature in Saccharomyces cerevisiae","authors":"Xianni Qi , Zhen Wang , Yuping Lin , Yufeng Guo , Zongjie Dai , Qinhong Wang","doi":"10.1016/j.engmic.2023.100108","DOIUrl":"10.1016/j.engmic.2023.100108","url":null,"abstract":"<div><p>Industrial manufacturing of bioproducts, especially bioethanol, can benefit from high-temperature fermentation, which requires the use of thermotolerant yeast strains. Mitochondrial activity in yeast is closely related to its overall metabolism. However, the mitochondrial respiratory changes in response to adaptive thermotolerance are still poorly understood and have been rarely utilized for developing thermotolerant yeast cell factories. Here, adaptive evolution and transcriptional sequencing, as well as whole-genome-level gene knockout, were used to obtain a thermotolerant strain of <em>Saccharomyces cerevisiae</em>. Furthermore, thermotolerance and bioethanol production efficiency of the engineered strain were examined. Physiological evaluation showed the boosted fermentation capacity and suppressed mitochondrial respiratory activity in the thermotolerant strain. The improved fermentation produced an increased supply of adenosine triphosphate required for more active energy-consuming pathways. Transcriptome analysis revealed significant changes in the expression of the genes involved in the mitochondrial respiratory chain. Evaluation of mitochondria-associated gene knockout confirmed that <em>ADK1, DOC1,</em> or <em>MET7</em> were the key factors for the adaptive evolution of thermotolerance in the engineered yeast strain. Intriguingly, overexpression of <em>DOC1</em> with <em>TEF1</em> promoter regulation led to a 10.1% increase in ethanol production at 42 °C. The relationships between thermotolerance, mitochondrial activity, and respiration were explored, and a thermotolerant yeast strain was developed by altering the expression of mitochondrial respiration-related genes. This study provides a better understanding on the physiological mechanism of adaptive evolution of thermotolerance in yeast.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 2","pages":"Article 100108"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370323000401/pdfft?md5=fc8f07d0ab59477e3894e1846ec85ed5&pid=1-s2.0-S2667370323000401-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135248195","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"O-methyltransferase CbzMT catalyzes iterative 3,4-dimethylations for carbazomycin biosynthesis","authors":"Baixin Lin, Dashan Zhang, Junbo Wang, Yongjian Qiao, Jinjin Wang, Zixin Deng, Lingxin Kong, Delin You","doi":"10.1016/j.engmic.2024.100150","DOIUrl":"10.1016/j.engmic.2024.100150","url":null,"abstract":"<div><p>Carbazomycins (<strong>1</strong>–<strong>8</strong>) are a subgroup of carbazole derivatives that contain oxygen at the C3 and C4 positions and an unusual asymmetric substitution pattern. Several of these compounds exhibit antifungal and antioxidant activities. To date, no systematic biosynthetic studies have been conducted on carbazomycins. In this study, carbazomycins A and B (<strong>1</strong> and <strong>2</strong>) were isolated from <em>Streptomyces luteosporeus</em> NRRL 2401 using a one-strain-many-compound (OSMAC)-guided natural product mining screen. A biosynthetic gene cluster (BGC) was identified, and possible biosynthetic pathways for <strong>1</strong> and <strong>2</strong> were proposed. The <em>in vivo</em> genetic manipulation of the O-methyltransferase-encoding gene <em>cbzMT</em> proved indispensable for <strong>1</strong> and <strong>2</strong> biosynthesis. Size exclusion chromatography indicated that CbzMT was active as a dimer. <em>In vitro</em> biochemical assays confirmed that CbzMT could repeatedly act on the hydroxyl groups at C3 and C4, producing monomethylated <strong>2</strong> and dimethylated <strong>1</strong>. Monomethylated carbazomycin B (<strong>2</strong>) is not easily methylated; however, CbzMT seemingly prefers the dimethylation of the dihydroxyl substrate (<strong>12</strong>) to <strong>1</strong>, even with a low conversion efficiency. These findings not only improve the understanding of carbazomycin biosynthesis but also expand the inventory of OMT-catalyzing iterative methylations on different acceptor sites, paving the way for engineering biocatalysts to synthesize new active carbazomycin derivatives.</p></div>","PeriodicalId":100478,"journal":{"name":"Engineering Microbiology","volume":"4 2","pages":"Article 100150"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667370324000134/pdfft?md5=3368a6d51be469c2d456f31ac0ae09eb&pid=1-s2.0-S2667370324000134-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140776534","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}