Preparative Biochemistry & Biotechnology最新文献_第10页

Proteases, a powerful biochemical tool in the service of medicine, clinical and pharmaceutical. 蛋白酶是为医学、临床和制药服务的强大生化工具。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-06-22 DOI: 10.1080/10826068.2024.2364234

Ghadir A Jamal, Ehsan Jahangirian, Michael R Hamblin, Hamed Mirzaei, Hossein Tarrahimofrad, Neda Alikowsarzadeh

{"title":"Proteases, a powerful biochemical tool in the service of medicine, clinical and pharmaceutical.","authors":"Ghadir A Jamal, Ehsan Jahangirian, Michael R Hamblin, Hamed Mirzaei, Hossein Tarrahimofrad, Neda Alikowsarzadeh","doi":"10.1080/10826068.2024.2364234","DOIUrl":"https://doi.org/10.1080/10826068.2024.2364234","url":null,"abstract":"Proteases, enzymes that hydrolyze peptide bonds, have various applications in medicine, clinical applications, and pharmaceutical development. They are used in cancer treatment, wound debridement, contact lens cleaning, prion degradation, biofilm removal, and fibrinolytic agents. Proteases are also crucial in cardiovascular disease treatment, emphasizing the need for safe, affordable, and effective fibrinolytic drugs. Proteolytic enzymes and protease biosensors are increasingly used in diagnostic and therapeutic applications. Advanced technologies, such as nanomaterials-based sensors, are being developed to enhance the sensitivity, specificity, and versatility of protease biosensors. These biosensors are becoming effective tools for disease detection due to their precision and rapidity. They can detect extracellular and intracellular proteases, as well as fluorescence-based methods for real-time and label-free detection of virus-related proteases. The active utilization of proteolytic enzymatic biosensors is expected to expand significantly in biomedical research, in-vitro model systems, and drug development. We focused on journal articles and books published in English between 1982 and 2024 for this study.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-25"},"PeriodicalIF":2.0,"publicationDate":"2024-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141440799","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Cellulase production by Aspergillus fumigatus A4112 and the potential use of the enzyme in cooperation with surfactant to enhance floating oil recovery and methane production from palm oil mill effluent. 烟曲霉 A4112 产生的纤维素酶以及该酶与表面活性剂合作用于提高棕榈油厂污水的浮油回收率和甲烷产量的潜力。

IF 2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-06-22 DOI: 10.1080/10826068.2024.2368627

Wiyada Khangkhachit, Wasana Suyotha, Sompong O-Thong, Poonsuk Prasertsan

{"title":"Cellulase production by Aspergillus fumigatus A4112 and the potential use of the enzyme in cooperation with surfactant to enhance floating oil recovery and methane production from palm oil mill effluent.","authors":"Wiyada Khangkhachit, Wasana Suyotha, Sompong O-Thong, Poonsuk Prasertsan","doi":"10.1080/10826068.2024.2368627","DOIUrl":"https://doi.org/10.1080/10826068.2024.2368627","url":null,"abstract":"This research performed cellulase production by Aspergillus fumigatus A4112 and evaluated its potential use in palm oil mill effluent (POME) hydrolysis to recover oil simultaneously with the generation of fermentable sugar useful for biofuel production under non-sterilized conditions. Empty fruit bunch (EFB) without pretreatment was used as carbon source. The combination of nitrogen sources facilitated CMCase production. The maximum activity (3.27 U/mL) was obtained by 1.0 g/L peptone and 1.5 g/L (NH4)2SO4 and 20 g/L EFB at 40 °C for 7 days. High level of FPase activity (39.51 U/mL) was also obtained. Interestingly, the enzyme retained its cellulase activities more than 60% at ambient temperature over 15 days. In enzymatic hydrolysis, Triton X-100 was an effective surfactant to increase total oil recovery in the floating form. High yield of reducing sugar (50.13 g/L) and 21% (v/v) of floating oil was recoverable at 65 °C for 48 h. Methane content of the raw POME increased from 41.49 to 64.94% by using de-oiled POME hydrolysate which was higher than using the POME hydrolysate (59.82%). The results demonstrate the feasibility of the constructed process for oil recovery coupled with a subsequent step for methane yield enhancement in biogas production process that benefits the palm oil industry.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-12"},"PeriodicalIF":2.0,"publicationDate":"2024-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141440798","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Comparative studies on modeling and optimization of fermentation process conditions for fungal asparaginase production using artificial intelligence and machine learning techniques 利用人工智能和机器学习技术对真菌天冬酰胺酶生产发酵工艺条件建模和优化的比较研究

IF 2.9 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-06-19 DOI: 10.1080/10826068.2024.2367692

Gurunathan Baskar, Rajendran Sivakumar, Seifedine Kadry, Cheng-Di Dong, Reeta Rani Singhania, Ramanujam Praveenkumar, Elumalai Raja Sathendra

引用次数: 0

Effects of fermentation on the structures of yellow compounds in citrus pomace. 发酵对柑橘渣中黄色化合物结构的影响。

IF 2.9 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-06-10 DOI: 10.1080/10826068.2024.2362794

Dan-Dan Yang, Wen-Jie Li, Sheng-Jiao Lei, Hai-Yan Liu, Nong-Fei Ouyang, Jun-Dong Zhu

引用次数: 0

Expression and characterization of a thermostable monoacylglycerol lipase from thermophilic Geobacillus kaustophilus. 嗜热革兰霉菌（Geobacillus kaustophilus）中一种恒温单酰基甘油脂肪酶的表达和特征。

IF 2.9 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-06-04 DOI: 10.1080/10826068.2024.2361147

Noriyuki Doukyu, Hayato Ito, Kugako Sugimoto

{"title":"Expression and characterization of a thermostable monoacylglycerol lipase from thermophilic Geobacillus kaustophilus.","authors":"Noriyuki Doukyu, Hayato Ito, Kugako Sugimoto","doi":"10.1080/10826068.2024.2361147","DOIUrl":"https://doi.org/10.1080/10826068.2024.2361147","url":null,"abstract":"Thermophilic Geobacillus kaustophilus HTA426 genome possesses a monoacylglycerol lipase (MAGL) gene. MAGLs can synthesize emulsifiers for use in the food and pharmaceutical industries from fatty acids and glycerol. They can also be used to analyze monoacylglycerol (MAG) levels in serum and food. The MAGL gene from strain HTA426 was artificially synthesized and heterologously expressed in Escherichia coli BL21(DE3). The recombinant His-tag fused MAGL (GkMAGL) was purified using a Ni2+-affinity column. The purified enzyme showed a temperature optimum at 65 °C and was stable up to 75 °C after 30 min incubation. In addition, the enzyme exhibited a pH optimum of 7.5 and was stable from pH 5.0 to 11.0. The enzyme hydrolyzed monoacylglycerols and showed the highest activity toward 1-monolauroylglycerol. The enzyme was stable in the presence of various organic solvents and detergents. The addition of Triton X-100 significantly increased GkMAGL activity. The thermal stability of the enzyme was higher than that of thermostable MAGL from Geobacillus sp. 12AMOR1 (12AMOR1_MAGL). Circular dichroism spectral analysis showed that the conformational stability of the GkMAGL was higher than that of 12AMOR1_MAGL at higher temperatures. These results indicate that the GkMAGL has useful features that can be used for various biotechnological applications.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-9"},"PeriodicalIF":2.9,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141238183","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

New wheat straw fermentation feed: recombinant Schizosaccharomyces pombe efficient degradation of lignocellulose and increase feed protein. 新型小麦秸秆发酵饲料：重组小麦酵母菌（Schizosaccharomyces pombe）高效降解木质纤维素并增加饲料蛋白质。

IF 2.9 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-06-02 DOI: 10.1080/10826068.2024.2353637

Xihua Chen, Xiaoyu Liang, Na Shi, Lu He, Yi Ma, Daochen Zhu, Zhong Ni, Huayou Chen

{"title":"New wheat straw fermentation feed: recombinant Schizosaccharomyces pombe efficient degradation of lignocellulose and increase feed protein.","authors":"Xihua Chen, Xiaoyu Liang, Na Shi, Lu He, Yi Ma, Daochen Zhu, Zhong Ni, Huayou Chen","doi":"10.1080/10826068.2024.2353637","DOIUrl":"https://doi.org/10.1080/10826068.2024.2353637","url":null,"abstract":"Wheat straw contains a high amount of lignin, hindering the action of cellulase and hemicellulase enzymes, leading to difficulties in nutrient absorption by animals from straw feed. However, currently, the biological treatment of straw relies primarily on fungal degradation and cannot be directly utilized for the preparation of livestock feed. This study focuses on enzymatic co-fermentation of wheat straw to produce high-protein, low-cellulose biological feed, integrating lignin degradation with feed manufacturing, thereby simplifying the feed production process. After the optimization using Box-Behnken Design for the feed formulation, with a glucose oxidase addition of 2.46%, laccase addition of 3.4%, and malonic acid addition of 0.6%, the wheat straw feed prepared in this experiment exhibited a true protein content of 9.35%. This represented a fourfold increase compared to the non-fermented state, and the lignocellulose degradation rate of wheat straw reached 45.42%. These results not only highlight the substantial enhancement in protein content but also underscore the significant advancement in lignocellulose breakdown. This formulation significantly enhanced the palatability and nutritional value of the straw feed, contributing to the industrial development of straw feed.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-9"},"PeriodicalIF":2.9,"publicationDate":"2024-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141186566","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Soluble and insoluble expression of recombinant human interleukin-2 protein using pET expression vector in Escherichia coli. 使用 pET 表达载体在大肠杆菌中可溶和不可溶地表达重组人白细胞介素-2 蛋白。

IF 2.9 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-06-02 DOI: 10.1080/10826068.2024.2361146

Atif Ahmed, Nao Akusa Fujimura, Saad Tahir, Muhammad Akram, Zaheer Abbas, Maira Riaz, Ali Raza, Rabia Abbas, Nadeem Ahmed

{"title":"Soluble and insoluble expression of recombinant human interleukin-2 protein using pET expression vector in Escherichia coli.","authors":"Atif Ahmed, Nao Akusa Fujimura, Saad Tahir, Muhammad Akram, Zaheer Abbas, Maira Riaz, Ali Raza, Rabia Abbas, Nadeem Ahmed","doi":"10.1080/10826068.2024.2361146","DOIUrl":"https://doi.org/10.1080/10826068.2024.2361146","url":null,"abstract":"Interleukin-2 has emerged as a potent protein-based drug to treat various cancers, AIDS, and autoimmune diseases. Despite its immense requirement, the production procedures are inefficient to meet the demand. Therefore, efficient production procedures must be adopted to improve protein yield and decrease procedural loss. This study analyzed cytoplasmic and periplasmic IL-2 expression for increased protein yield and significant biological activity. The study is focused on cloning IL-2 into a pET-SUMO and pET-28a vector that expresses IL-2 in soluble form and inclusion bodies, respectively. Both constructs were expressed into different E. coli expression strains, but the periplasmic and cytoplasmic expression of IL-2 was highest in overnight culture in Rosetta 2 (DE3). Therefore, E. coli Rosetta 2 (DE3) was selected for large-scale production and purification. Purified IL-2 was characterized by SDS-PAGE and western blotting, while its biological activity was determined using MTT bioassay. The results depict that the periplasmic and cytoplasmic IL-2 achieved adequate purification, yielding 0.86 and 0.51 mg/mL, respectively, with significant cytotoxic activity of periplasmic and cytoplasmic IL-2. Periplasmic IL-2 has shown better yield and significant biological activity in vitro which describes its attainment of native protein structure and function.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-13"},"PeriodicalIF":2.9,"publicationDate":"2024-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141186631","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Exploring traditional and modern approaches for extracting bioactive compounds from Ferulago trachycarpa. 探索从阿魏（Ferulago trachycarpa）中提取生物活性化合物的传统和现代方法。

IF 2.9 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-05-17 DOI: 10.1080/10826068.2024.2349937

Shakeel Ahmed, Nilofar, Aleksandra Cvetanović Kljakić, Alena Stupar, Biljana Lončar, Jelena Božunović, Uroš Gašić, Evren Yıldıztugay, Claudio Ferrante, Gokhan Zengin

{"title":"Exploring traditional and modern approaches for extracting bioactive compounds from Ferulago trachycarpa.","authors":"Shakeel Ahmed, Nilofar, Aleksandra Cvetanović Kljakić, Alena Stupar, Biljana Lončar, Jelena Božunović, Uroš Gašić, Evren Yıldıztugay, Claudio Ferrante, Gokhan Zengin","doi":"10.1080/10826068.2024.2349937","DOIUrl":"https://doi.org/10.1080/10826068.2024.2349937","url":null,"abstract":"For more than two millennia, Ferulago species have been revered as therapeutic herbs, maintaining their significance in present-day folk medicine practices. Therefore, the present study was conducted to investigate the phytochemical composition, inhibitory effects on metabolic enzymes, and possible therapeutic applications of F. trachycarpa, specifically focusing on its efficacy in diabetes management, anticholinergic effects, and antioxidant capabilities. The current investigation comprised an evaluation of a range of extracts acquired via conventional and modern methodologies, such as soxhlet (SOX), maceration (MAC) accelerated solvent extraction (ASE), homogenizer-assisted extraction (HAE), supercritical fluid extraction (SFE), microwave-assisted extraction (MW), and ultrasound-assisted extraction (UAE). Various techniques were employed to assess their antioxidant capacity and enzyme inhibition. Furthermore, the research utilized ultra-high performance liquid chromatography-MS/MS (UHPLC-MS/MS) to ascertain the principal phenolic compounds that are responsible for the antioxidant capacity observed in the various F. trachycarpa extracts. Among these, extracts from HAE, ASE, and MW revealed the most promise across all methodologies tested for their antioxidant potential. Furthermore, SFE and MAC extracts inhibited the most enzymes, including cholinesterases, tyrosinase, α -amylase, and α -glycosidase, indicating their potential as efficient natural treatments for several health-related issues.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-14"},"PeriodicalIF":2.9,"publicationDate":"2024-05-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140959020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Production, characterization, and bio-ethanologenic potential of a novel tripartite raw starch-digesting amylase from Priestia flexa UCCM 00132. 一种新的三元原料淀粉消化淀粉酶的生产、表征和生物产乙醇潜力。

IF 2.9 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-05-01 Epub Date: 2023-10-03 DOI: 10.1080/10826068.2023.2259452

David Sam Ubi, Maurice George Ekpenyong, Eloghosa Joyce Ikharia, Ernest Ablewho Akwagiobe, Atim David Asitok, Sylvester Peter Antai

{"title":"Production, characterization, and bio-ethanologenic potential of a novel tripartite raw starch-digesting amylase from Priestia flexa UCCM 00132.","authors":"David Sam Ubi, Maurice George Ekpenyong, Eloghosa Joyce Ikharia, Ernest Ablewho Akwagiobe, Atim David Asitok, Sylvester Peter Antai","doi":"10.1080/10826068.2023.2259452","DOIUrl":"10.1080/10826068.2023.2259452","url":null,"abstract":"The biological conversion of agro-waste biomass into value-added metabolites is one of the trendy biotechnological research areas in recent times. One of the major drawbacks of the bioprocess is the saccharification potential of the amylolytic enzyme that releases reducing sugar from complex biomass to serve as substrate for fermentation. The present study reports the production of a novel tripartite raw starch-digesting amylase (RSDA) by an indigenous Priestia flexa strain with α-, β-, and gluco-amylolytic activities and its potential for bioethanol production. Response surface statistics was employed to develop a suitable medium for improved production of the tripartite enzyme by submerged fermentation. The bioprocess selected raw starch (4.36%) Ca2+(2.71 g/L) and Zn2+ (0.0177 g/L) as significant variables which demonstrated a total RSDA activity of 7208.23 U/mL in a 5-L batch bioreactor. SDS/Native-PAGE determined the molecular weights of the 27-fold purified product as 25.2 kDa, 57.3 kDa, and 90.1 kDa for α-, β-, and gluco-amylases, respectively. Optimum temperature and pH for enzyme activity were respectively broad at 30-70 °C and 4-11. The enzyme mixture demonstrated digestibility above 90% against a variety of raw starches and simultaneous fermentation of digestate with Saccharomyces cerevisiae generated 71.69 g/L of bioethanol within 24 h suggesting great potential for bioethanologenesis.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"597-611"},"PeriodicalIF":2.9,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41140550","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Extraction of collagenolytic proteases from Aspergillus heteromorphus URM 0269 in an aqueous two-phase system for application in collagen hydrolysis. 在双水相系统中从异形曲霉URM 0269中提取胶原分解蛋白酶用于胶原水解。

IF 2.9 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2024-05-01 Epub Date: 2023-10-10 DOI: 10.1080/10826068.2023.2263870

Beatriz de Aquino Marques da Costa, Ana Cláudia Vaz de Araújo, Lígia Maria Gonçalves Fernandes, Ana Lúcia Figueiredo Porto, Vagne de Melo Oliveira, Tatiana Souza Porto

{"title":"Extraction of collagenolytic proteases from Aspergillus heteromorphus URM 0269 in an aqueous two-phase system for application in collagen hydrolysis.","authors":"Beatriz de Aquino Marques da Costa, Ana Cláudia Vaz de Araújo, Lígia Maria Gonçalves Fernandes, Ana Lúcia Figueiredo Porto, Vagne de Melo Oliveira, Tatiana Souza Porto","doi":"10.1080/10826068.2023.2263870","DOIUrl":"10.1080/10826068.2023.2263870","url":null,"abstract":"Collagenolytic proteases produced by Aspergillus heteromorphus URM0269 were extracted using a PEG/sulfate aqueous two-phase system (ATPS). A 23 factorial design was performed to analyze the independent variables: PEG molar mass (MPEG), PEG concentration (CPEG), and sulfate concentration (Csulf). The extracted proteases were also evaluated for their optimum pH and stability at different pH levels (4.0 - 11.0) after 20 h of incubation. Collagen was extracted from mutton snapper (Lutjanus analis) skin using acetic acid (0.5 mol L-1). The enzyme was preferentially partitioned to the PEG-rich phase (K > 1), whose highest purification factor and recovery (PF = 6.256 and Y = 404.432%) were obtained under specific conditions: MPEG 8000 g.mol-1, CPEG 30%, Csulf 10%. The ATPS extraction provided an enzymatic activity range of pH 7.0 - 11.0, exhibiting greater stability compared to the crude extract. Approximately 80% of protease activity was maintained after 20 hours of incubation at all analyzed pH levels, except pH 11.0. Collagen extraction from L. analis skin yielded 8.056%, and both crude extract samples and ATPS-derived samples successfully hydrolyzed the extracted collagen, reaching peak hydrolysis after 36 hours of treatment. These findings demonstrate the feasibility of extracting highly purified and active proteases capable of hydrolyzing L. analis collagen.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"647-659"},"PeriodicalIF":2.9,"publicationDate":"2024-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41183393","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0