Enzyme and Microbial Technology最新文献

{"title":"Corrigendum to “Effects of overexpression of the human intestinal alkaline phosphatase gene on the expression of related genes in intestinal epithelium-like cells” [Enzyme Microb. Technol. 195 (2026) 110807]","authors":"Seiko Noda , Shiho Ishii , Asako Yamada , Sadako Matsui , Hideo Orimo , Masae Goseki-Sone","doi":"10.1016/j.enzmictec.2026.110820","DOIUrl":"10.1016/j.enzmictec.2026.110820","url":null,"abstract":"","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110820"},"PeriodicalIF":3.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146044006","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":"Naringinase: A comprehensive review on its characteristics, production, and biotechnological applications","authors":"Nidhi S. Hallikeri ,&nbsp;Deepak A. Yaraguppi ,&nbsp;Bhavya S. Gangadharappa ,&nbsp;Nitin Mantri","doi":"10.1016/j.enzmictec.2025.110808","DOIUrl":"10.1016/j.enzmictec.2025.110808","url":null,"abstract":"<div><div>Naringinase is a bifunctional enzyme exhibiting both α-<span>L</span>-rhamnosidase and β-<span>D</span>-glucosidase activity, primarily utilized for the hydrolysis of bitter compounds like naringin in citrus products. This enzymatic action yields naringenin, a bioactive flavonoid known for its significant antioxidant, anti-inflammatory, and cardioprotective properties. Given its dual enzymatic function and substrate specificity, naringinase has garnered substantial interest across the food, pharmaceutical, and broader biotechnological sectors. This comprehensive review critically examines recent advancements concerning naringinase, focusing on its microbial production, optimization strategies in fermentation, purification methods, and various immobilization technologies. <em>Aspergillus niger</em> and <em>Penicillium decumbens</em> are identified as the predominant microbial sources for naringinase production, with solid-state fermentation demonstrating economic and cost-effectiveness over submerged fermentation. The application of diverse immobilization techniques, including adsorption, covalent binding, and encapsulation, has been shown to significantly enhance the enzyme's catalytic stability, reusability, and overall efficiency in applications such as juice debittering and the development of functional foods. While advanced biocatalysis approaches like recombinant expression and enzyme engineering offer promising improvements in catalytic properties, the persistent challenges related to production scalability and purification costs warrant further assessment. The integration of sustainable solid-state fermentation with cutting-edge nanomaterials holds considerable promise, opening new avenues for naringinase applications in environmental biotechnology and personalized medicine.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110808"},"PeriodicalIF":3.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145877903","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":"Cellulose biosynthesis in nature and In Vitro: mechanisms and challenges","authors":"Shijing Sun ,&nbsp;Huasha Liang ,&nbsp;Zehai Lei ,&nbsp;Jialei Xu ,&nbsp;Siqi Wang ,&nbsp;Zhongyuan Zhao ,&nbsp;Tongming Yin","doi":"10.1016/j.enzmictec.2025.110804","DOIUrl":"10.1016/j.enzmictec.2025.110804","url":null,"abstract":"<div><div>This review systematically compares the biosynthetic mechanisms of cellulose in plants and bacteria, focusing on the structure and function of their distinct enzymatic complexes. In bacteria, cellulose synthesis is driven by the BcsAB transmembrane complex alongside auxiliary proteins like BcsC and BcsD. In plants, rosette-shaped cellulose synthase complexes (CSCs), which are composed of multiple CesA catalytic subunits, synthesize cellulose microfibrils. This process is critically coordinated by auxiliary proteins, such as KOR1 and COBRA-LIKE proteins, which associate with or regulate the CSCs to ensure proper microfibril formation and crystallization. A central challenge in the field is the <em>in vitro</em> production of cellulose I, the native crystalline form with superior mechanical properties. While strategies such as enzyme extraction and heterologous expression in <em>Escherichia coli</em> enable cellulose production, they typically yield the less desirable cellulose II allomorph and face issues of low yield and instability. This review synthesizes current knowledge on key enzymes, <em>in vitro</em> synthesis methods, and resulting cellulose characteristics to identify key obstacles and future pathways toward the efficient bio-manufacturing of cellulose I for sustainable applications.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110804"},"PeriodicalIF":3.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145881448","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":"Effects of overexpression of the human intestinal alkaline phosphatase gene on the expression of related genes in intestinal epithelium-like cells","authors":"Seiko Noda ,&nbsp;Shiho Ishii ,&nbsp;Asako Yamada ,&nbsp;Sadako Matsui ,&nbsp;Hideo Orimo ,&nbsp;Masae Goseki-Sone","doi":"10.1016/j.enzmictec.2025.110807","DOIUrl":"10.1016/j.enzmictec.2025.110807","url":null,"abstract":"<div><div>Alkaline phosphatase is an enzyme that hydrolyzes phosphate monoesters. Intestinal-type ALP (IAP), which localizes to the small intestine, is closely associated with dietary factors; however, its physiological functions remain largely unclear. Therefore, we herein hypothesized that the transient overexpression of the human <em>Intestinal Alkaline Phosphatase</em> (<em>ALPI</em>) gene, which encodes IAP, may suggest its effects on the expression of other related genes. Human intestinal epithelium-like Caco-2 cells were transfected with an IAP expression vector or a Mock control to induce transient overexpression. Three days later, Caco-2 cells were harvested and RNA was extracted. Using purified RNA, a comprehensive gene expression analysis was performed by RNA sequencing with next-generation sequencing technology. In comparisons with the Mock control, 1036 differentially expressed genes (DEGs) were identified in Caco-2 cells transfected with the human IAP expression vector. The expression of 79 of these genes was more than two-fold higher, while that of 74 of these genes was more than two-fold lower. The GO analysis of the 79 up-regulated genes demonstrated that seven genes were enriched in “nervous system development” and three genes in “negative chemotaxis”. In contrast, the GO analysis of the 74 down-regulated genes demonstrated that two genes were enriched in “membrane repolarization during atrial cardiac muscle cell action potential”, four genes in “cell surface receptor signaling pathway”, five genes were enriched in “neuron projection”, and three genes in “perikaryon”. Further studies are warranted to investigate the relationships between DEGs and the regulation of <em>ALPI</em> gene expression in more detail.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110807"},"PeriodicalIF":3.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145881449","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 activity and stability of thermostable endoglucanase Dictyoglomus turgidum DtCelA with multiple strategies","authors":"Xiaotong Kang ,&nbsp;Hang Yuan ,&nbsp;Weimeng Li,&nbsp;Yun Hu,&nbsp;Fubao Sun","doi":"10.1016/j.enzmictec.2025.110809","DOIUrl":"10.1016/j.enzmictec.2025.110809","url":null,"abstract":"<div><div>Thermophilic endoglucanases are of big promise in enzymatic degradation of lignocellulosic substrate, yet their limited catalytic efficiency remains a major barrier to industrial application. This study focused on the improvement of activity and stability of thermostable endoglucanase <em>Dt</em>CelA from <em>Dictyoglomus turgidum</em> with a three-stage cascade engineering strategy that integrated model-guided site-directed mutagenesis, disulfide bond introduction, and carbohydrate-binding module (CBM) fusion. Among the variants, the triple mutant S25D/T265C/A305C fused with CBM2 (S25D/T265C/A305C-A-CBM2) exhibited a 90.56 % increase in specific activity toward CMC relative to the wild type, together with a 2.97-fold longer half-life at 75 °C and a 5.3-fold longer at 80 °C. This mutant also displayed 3.0- and 5.4-fold higher hydrolytic activity against Avicel and konjac glucomannan, respectively. On natural lignocellulosic substrates including filter paper, sugarcane bagasse, and corn stover, the mutant also showed potential application. The mutated endoglucanase <em>Dt</em>CelA was powerful with enhanced catalytic performance and thermostability after multicascade engineering, which can provide a robust framework for the rational design of cellulases that are optimized for high-temperature biorefinery process.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110809"},"PeriodicalIF":3.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145862488","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":"Harnessing enzyme and microbial biotechnology for macroalgae valorization: A circular economy approach with implications for carbon sequestration","authors":"Bharmjeet Singh ,&nbsp;Mahesh Vemula ,&nbsp;Abeba Haile Mariamenatu ,&nbsp;Abdalah Makaranga ,&nbsp;Asha Arumugam Nesamma ,&nbsp;Pannaga Pavan Jutur","doi":"10.1016/j.enzmictec.2026.110819","DOIUrl":"10.1016/j.enzmictec.2026.110819","url":null,"abstract":"<div><div>Macroalgae are a sustainable, non-terrestrial biomass resource critical for the emerging blue economy. They play a crucial role in marine ecosystems, including the natural sequestration of carbon, which grounds the entire value chain in sustainable CO₂ removal. This review presents how enzyme and microbial biotechnology drive the techno-economic feasibility of macroalgal processing within a circular biorefinery framework. We detail how tailored enzymatic cocktails enable the selective, mild-condition extraction and modification of high-value, mainstream products, such as hydrocolloids and nutraceuticals like omega-3 lipids, from the three major macroalgal groups. Concurrently, microbial bioconversion is crucial for transforming macroalgal components, including polysaccharides, proteins, and lipids, into byproducts such as biofuels and biofertilizers, thereby ensuring resource efficiency and minimizing waste. The application of molecular omics technologies (genomics, transcriptomics, proteomics, and metabolomics) is shown to underpin the macroalgal biology and optimize bioprocesses by identifying novel microbial strains, enzymes and engineering metabolic pathways of microbial strains to enhance yields and specificity. The study addresses technological, economic, and environmental difficulties. This integrated, cascading approach is necessary to transition macroalgae valorization from single-product extraction to a profitable, multi-product industry, balancing economic growth with environmental preservation. Critical assessment of the framework's overall environmental viability relies on life cycle analysis (LCA). This review contributes an essential methodological synthesis to guide future studies, ensuring consistent sustainability assessment of the macroalgal biorefinery.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110819"},"PeriodicalIF":3.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146009097","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":"Integrated bio-nano remediation of produced water using Alcanivorax borkumensis and GQDs-modified ZnO/La₂O₃ nanocomposites","authors":"Tahseen Hameed Khlaif","doi":"10.1016/j.enzmictec.2025.110810","DOIUrl":"10.1016/j.enzmictec.2025.110810","url":null,"abstract":"<div><div>This study presents a novel, synergistic bioremediation platform for petroleum-contaminated produced water, utilizing <em>Alcanivorax borkumensis</em> in conjunction with a hybrid nanocomposite of graphene quantum dots (GQDs), zinc oxide (ZnO), and lanthanum oxide (La₂O₃). The nanocomposite was synthesized via ultrasonic-assisted co-precipitation and hydrothermal methods, exhibiting high surface area and photocatalytic potential. The bacterium was isolated from oil-field equipment and identified based on 16S rRNA sequencing, showing selective affinity for hydrocarbons in saline conditions. Integrated systems were optimized by evaluating nanocomposite dose, contact time, and light intensity. Results revealed a clear synergy: GQDs enhanced bacterial adhesion and minimized cytotoxicity, while ZnO/La₂O₃ contributed to robust radical formation under light exposure. Combined systems achieved over 98 % total petroleum hydrocarbon (TPH) and 99 % polycyclic aromatic hydrocarbon (PAH) removal, outperforming individual components. Material characterizations (BET, FTIR, XRD, SEM) confirmed the composite’s stability and biointerface compatibility. Comparative trials across bacteria-only, nanomaterial-only, and hybrid systems validated the superiority of the bio-nanocomposite configuration. The approach merges enzymatic and photocatalytic degradation in a biologically resilient matrix, providing a scalable, environmentally sound strategy for industrial water treatment. These findings offer a comprehensive framework for future application of microbe–nanomaterial hybrids in complex pollutant removal.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110810"},"PeriodicalIF":3.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145881384","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":"Dithionite-supported biohydrogenation of muconic acid to adipic acid by lyophilized Escherichia coli cells expressing recombinant enoate reductase","authors":"Khorcheska A. Batyrova ,&nbsp;Anna N. Khusnutdinova ,&nbsp;Alexander F. Yakunin","doi":"10.1016/j.enzmictec.2025.110797","DOIUrl":"10.1016/j.enzmictec.2025.110797","url":null,"abstract":"<div><div>Adipic acid is an important six-carbon dicarboxylic acid with numerous industrial applications in polymers (nylon) and the food industry. Traditional manufacturing of adipic acid relies on petroleum feedstocks and involves energy-intensive chemical processes with negative environmental impacts. Consequently, alternative synthesis methods are being developed, including the hydrogenation of biobased muconic acid to adipic acid via chemical catalysis or enzymatic reduction with 2-enoate reductases. This study revealed that purified full-length 2-enoate reductase ERBC from <em>Heyndrickxia</em> (<em>Bacillus</em>) <em>coagulans</em> can reduce the three muconic acid isomers (<em>cis,cis</em>, <em>cis,trans</em>, <em>trans,trans</em>) using NADH as a reductant. Titration of the purified ERBC with different chemical reductants showed that its redox cofactors (FMN, FAD, and [4Fe-4S]) can also be reduced by dithionite and Ti(III)-citrate. However, only dithionite and NADH supported the biohydrogenation of <em>trans</em>-cinnamic acid and <em>cis,cis</em>-muconic acid. The individually expressed and purified large domain of ERBC also catalyzed muconic acid reduction with these reductants, but exhibited lower activity and produced only 2-hexenedioic acid as the product. Efficient conversion of muconic acid to adipic acid was demonstrated using lyophilized <em>E. coli</em> cells expressing full-length ERBC as the catalyst, with dithionite acting as both a reductant and an oxygen scavenger. The use of lyophilized recombinant <em>Escherichia coli</em> cells with dithionite for ERBC-mediated biohydrogenation of muconic acid eliminates the need for protein purification and costly natural cofactors (NAD(P)H), as well as enhances ERBC tolerance to high substrate concentrations and creates anaerobic conditions for ERBC activity. This approach shows promise for biobased adipic acid production and other applications of 2-enoate reductases.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"194 ","pages":"Article 110797"},"PeriodicalIF":3.7,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145676679","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 degradation of thermoplastic polyurethane plastics based on engineering lignin peroxidase","authors":"Huan Li,&nbsp;Shengjie Yuan,&nbsp;Ling Chen,&nbsp;Bing Wu","doi":"10.1016/j.enzmictec.2025.110788","DOIUrl":"10.1016/j.enzmictec.2025.110788","url":null,"abstract":"<div><div>Thermoplastic polyurethane (TPU) with complex physical crosslinking is difficult to degrade under natural environmental conditions. Current degradation methods, particularly for aromatic TPU, suffer from poor degradation efficiency. This study investigated the degradation performance of lignin peroxidase (LiP) on aromatic TPU through protein engineering and multi-enzyme system construction. Results indicated that wild-type LiP (WT-LiP), expressed from the recombinant <em>Pichia pastoris</em> GS115, exhibited a certain degradation effect on aromatic TPU. By using molecular docking techniques to identify key mutation sites, three LiP mutants (F46W, H47W, and H175R) were successfully constructed. Under optimal conditions (30°C, pH 2.5, 1 mM H₂O₂, and 5 U/mg enzyme), the F46W mutant achieved a molecular weight degradation rate of 11.97 % after 3 days of degradation, which is 2.2 times higher than that of the WT-LiP with a weight loss of 2.22 %, and the degradation efficiency in 28 days was 26.59 %. Furthermore, the constructed multi-enzyme systems (LiP-manganese peroxidase-laccase and LiP-carboxylesterase) substantially improved the degradation efficiency of TPU. Specifically, the LiP-carboxylesterase system demonstrated superior performance, achieving molecular weight degradation rates of 29.20 % and weight loss of 5.07 % after 3 days of treatment. This study provides a green enzymatic approach for efficient aromatic TPU plastics degradation and offers more sustainable solutions for plastic waste management.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"194 ","pages":"Article 110788"},"PeriodicalIF":3.7,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145622365","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":"Overexpression of Keratinase Candidate from Bacillus velezensis LPL061 in Escherichia coli BL21(DE3)","authors":"Desi Sagita ,&nbsp;Tirza Jeli Ping ,&nbsp;Aluicia Anita Artarini ,&nbsp;Rachmat Mauluddin ,&nbsp;Edwin Setiawan ,&nbsp;Anto Budiharjo ,&nbsp;Catur Riani","doi":"10.1016/j.enzmictec.2025.110789","DOIUrl":"10.1016/j.enzmictec.2025.110789","url":null,"abstract":"<div><div>Proteases have diverse industrial applications including keratinase, which degrade keratin-rich substrates, such as hair, nails, feathers, and skin. This study aimed to express a protease of <em>Bacillus velezensis</em> LPL061 (WP_003155195.1) in <em>Escherichia coli</em> BL21(DE3) and to evaluate its keratinolytic as a new source of keratinase. Two gene constructs were designed, one containing the propeptide domain (<em>kerfull</em>) and one without it (<em>kerhalf</em>). Expression was induced with 0.05 mM IPTG at 20°C for 20 h. KerFull was partially purified using sequential ultrafiltration. SDS-PAGE analysis showed that KerHalf as a 32.2 kDa protein, while KerFull appeared as a 38 kDa fusion and a 28.5 kDa mature form. QTOF-MS confirmed the amino acid sequence. Only KerFull exhibited proteolytic and keratinolytic, highlighting the importance of the I9 domain for proper folding and enzyme activation. The partially purified mature KerFull protein (P50 fraction) retained activity despite low yield. KerFull showed a broad pH stability (6−11) with optimum at pH 9 and active over a wide temperature range (37–70℃), with an optimum at 60℃. Protein remained stable at 20–40℃ and pH 8. Specific activity reached 16.67 U/mg in the crude and 34.14 U/mg of P50 fraction. When combined with DTT, KerFull effectively degraded chicken feather barbules within 4 h at 37 °C. These findings suggest that one of the proteases from <em>B. velezensis</em> LPL061 (WP_003155195.1) is a robust keratinase candidate, offering broad operational pH and temperature, and efficient keratin degradation even at low concentrations, making it a promising candidate for industrial keratinase applications.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"194 ","pages":"Article 110789"},"PeriodicalIF":3.7,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145622366","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}