Journal of applied glycoscience最新文献_第3页

Identification and Characterization of Dextran α-1,2-Debranching Enzyme from Microbacterium dextranolyticum. 葡聚糖α-1,2-脱支酶的鉴定与表征

IF 1.1

Journal of applied glycoscience Pub Date : 2023-01-01 DOI: 10.5458/jag.jag.JAG-2022_0013

Takatsugu Miyazaki, Hidekazu Tanaka, Shuntaro Nakamura, Hideo Dohra, Kazumi Funane

{"title":"Identification and Characterization of Dextran α-1,2-Debranching Enzyme from Microbacterium dextranolyticum.","authors":"Takatsugu Miyazaki, Hidekazu Tanaka, Shuntaro Nakamura, Hideo Dohra, Kazumi Funane","doi":"10.5458/jag.jag.JAG-2022_0013","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0013","url":null,"abstract":"Dextran α-1,2-debranching enzyme (DDE) releases glucose with hydrolyzing α-(1→2)-glucosidic linkages in α-glucans, which are made up of dextran with α-(1→2)-branches and are generated by Leuconostoc bacteria. DDE was isolated from Microbacterium dextranolyticum (formerly known as Flavobacterium sp. M-73) 40 years ago, although the amino acid sequence of the enzyme has not been determined. Herein, we found a gene for this enzyme based on the partial amino acid sequences from native DDE and characterized the recombinant enzyme. DDE had a signal peptide, a glycoside hydrolase family 65 domain, a carbohydrate-binding module family 35 domain, a domain (D-domain) similar to the C-terminal domain of Arthrobacter globiformis glucodextranase, and a transmembrane region at the C-terminus. Recombinant DDE released glucose from α-(1→2)-branched α-glucans produced by Leuconostoc citreum strains B-1299, S-32, and S-64 and showed weak hydrolytic activity with kojibiose and kojitriose. No activity was detected for commercial dextran and Leuconostoc citreum B-1355 α-glucan, which do not contain α-(1→2)-linkages. The removal of the D-domain decreased the affinity for α-(1→2)-branched α-glucans but not for kojioligosaccharides, suggesting that D-domain plays a role in α-glucan binding. Genes for putative dextranases, oligo-1,6-glucosidase, sugar-binding protein, and permease were present in the vicinity of the DDE gene, and as a result these gene products may be necessary for the use of α-(1→2)-branched glucans. Our findings shed new light on how actinobacteria utilize polysaccharides produced by lactic acid bacteria.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f7/3b/70_jag.JAG-2022_0013.PMC10074034.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9272442","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}

引用次数: 0

Function and Structure of Lacticaseibacillus casei GH35 β-Galactosidase LBCZ_0230 with High Hydrolytic Activity to Lacto-N-biose I and Galacto-N-biose. 对乳糖- n -二糖I和乳糖- n -二糖具有高水解活性的干酪乳杆菌GH35 β-半乳糖苷酶LBCZ_0230的功能和结构

IF 1.1

Journal of applied glycoscience Pub Date : 2023-01-01 DOI: 10.5458/jag.jag.JAG-2022_0014

Wataru Saburi, Tomoya Ota, Koji Kato, Takayoshi Tagami, Keitaro Yamashita, Min Yao, Haruhide Mori

{"title":"Function and Structure of Lacticaseibacillus casei GH35 β-Galactosidase LBCZ_0230 with High Hydrolytic Activity to Lacto-N-biose I and Galacto-N-biose.","authors":"Wataru Saburi, Tomoya Ota, Koji Kato, Takayoshi Tagami, Keitaro Yamashita, Min Yao, Haruhide Mori","doi":"10.5458/jag.jag.JAG-2022_0014","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0014","url":null,"abstract":"β-Galactosidase (EC 3.2.1.23) hydrolyzes β-D-galactosidic linkages at the non-reducing end of substrates to produce β-D-galactose. Lacticaseibacillus casei is one of the most widely utilized probiotic species of lactobacilli. It possesses a putative β-galactosidase belonging to glycoside hydrolase family 35 (GH35). This enzyme is encoded by the gene included in the gene cluster for utilization of lacto-N-biose I (LNB; Galβ1-3GlcNAc) and galacto-N-biose (GNB; Galβ1-3GalNAc) via the phosphoenolpyruvate: sugar phosphotransferase system. The GH35 protein (GnbG) from L. casei BL23 is predicted to be 6-phospho-β-galactosidase (EC 3.2.1.85). However, its 6-phospho-β-galactosidase activity has not yet been examined, whereas its hydrolytic activity against LNB and GNB has been demonstrated. In this study, L. casei JCM1134 LBCZ_0230, homologous to GnbG, was characterized enzymatically and structurally. A recombinant LBCZ_0230, produced in Escherichia coli, exhibited high hydrolytic activity toward o-nitrophenyl β-D-galactopyranoside, p-nitrophenyl β-D-galactopyranoside, LNB, and GNB, but not toward o-nitrophenyl 6-phospho-β-D-galactopyranoside. Crystal structure analysis indicates that the structure of subsite -1 of LBCZ_0230 is very similar to that of Streptococcus pneumoniae β-galactosidase BgaC and not suitable for binding to 6-phospho-β-D-galactopyranoside. These biochemical and structural analyses indicate that LBCZ_0230 is a β-galactosidase. According to the prediction of LNB's binding mode, aromatic residues, Trp190, Trp240, Trp243, Phe244, and Tyr458, form hydrophobic interactions with N-acetyl-D-glucosamine residue of LNB at subsite +1.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/93/39/70_jag.JAG-2022_0014.PMC10432377.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10404620","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}

引用次数: 0

Effect of Water Vapor Sorption on Complex Formation in Amylose-lauric Acid Blend Powder. 水蒸气吸附对直链淀粉-月桂酸混合粉中络合物形成的影响。

IF 1.1

Journal of applied glycoscience Pub Date : 2023-01-01 DOI: 10.5458/jag.jag.JAG-2023_0001

Yuki Yoshitomi, Kiyoshi Kawai

{"title":"Effect of Water Vapor Sorption on Complex Formation in Amylose-lauric Acid Blend Powder.","authors":"Yuki Yoshitomi, Kiyoshi Kawai","doi":"10.5458/jag.jag.JAG-2023_0001","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2023_0001","url":null,"abstract":"The purpose of this study was to understand the effect of relative humidity (RH) on amylose-lipid complex (ALC) formation in amylose-lauric acid blend powder held at 50 °C (temperature slightly higher than the melting point of lauric acid) using differential scanning calorimetry (DSC) and X-ray diffraction. From DSC curves, the melting of crystalized lauric acid and two melting peaks of ALC were observed depending on RH. ALC formation was confirmed by X-ray diffraction pattern. The melting enthalpy (∆Hm) of lauric acid in the sample held at RH 0 % was lower than that of lauric acid only though there was no ALC formation. This suggests that crystallization of lauric acid was prevented by amylose. The ∆Hm of lauric acid increased with an increase in RH up to 79.0 % because liquid lauric acid would have fused as the result of enhanced repulsive force between liquid lauric acid and hydrated amylose. The ∆Hm of ALC increased with an increase in RH between 79.0 and 95.0 %. For ALC formation, amylose has to be mobile in the system, but dehydrated amylose is in a glassy (immobilize) state. According to the glass to rubber transition behavior of amorphous polymer, amylose held at 50 °C is suggested to become rubbery (mobile) state at RH 76.0 %. This interpretation will explain the reason why ALC formation began to be observed at the RH range between 72.4 and 79.0 %.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/65/a9/70_jag.JAG-2023_0001.PMC10432376.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10423718","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}

引用次数: 0

Molecular Weight Distribution of Whole Starch in Rice Endosperm by Gel-permeation Chromatography. 凝胶渗透色谱法研究水稻胚乳中全淀粉的分子量分布。

IF 1.1

Journal of applied glycoscience Pub Date : 2023-01-01 DOI: 10.5458/jag.jag.JAG-2022_0010

Naoto Suzuki, Isao Hanashiro, Naoko Fujita

引用次数: 2

Hyaluronidase-inhibiting Polysaccharide from Caulerpa lentillifera. 小扁豆透明质酸酶抑制多糖。

IF 1.1

Journal of applied glycoscience Pub Date : 2023-01-01 DOI: 10.5458/jag.jag.JAG-2022_0004

Mahanama Geegana Gamage Awanthi, Saki Nagamoto, Hirosuke Oku, Kanefumi Kitahara, Teruko Konishi

引用次数: 1

Automatic Calculation of the Kinetic Parameters of Enzymatic Reactions with Their Standard Errors Using Microsoft Excel. 用Microsoft Excel自动计算酶促反应动力学参数及其标准误差。

IF 1.1

Journal of applied glycoscience Pub Date : 2023-01-01 DOI: 10.5458/jag.jag.JAG-2022_0012

Motomitsu Kitaoka

引用次数: 2

Characterization of an α-L-Arabinofuranosidase GH51 from the Brown-rot Fungus Gloeophyllum trabeum. 褐腐菌中α- l -阿拉伯糖醛酸苷酶GH51的鉴定

IF 1.1

Journal of applied glycoscience Pub Date : 2023-01-01 DOI: 10.5458/jag.jag.JAG-2022_0009

Rikako Tsukida, Makoto Yoshida, Satoshi Kaneko

{"title":"Characterization of an α-L-Arabinofuranosidase GH51 from the Brown-rot Fungus Gloeophyllum trabeum.","authors":"Rikako Tsukida, Makoto Yoshida, Satoshi Kaneko","doi":"10.5458/jag.jag.JAG-2022_0009","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0009","url":null,"abstract":"Woody biomass is anticipated to be a resource for a decarbonized society, but the difficulty of isolating woody components is a significant challenge. Brown-rot fungi, a type of wood rotting fungi, decompose hemicellulose particularly efficiently. However, there are few reports on the hemicellulases from brown-rot fungi. An α-L-arabinofuranosidase belonging to glycoside hydrolase family 51 (GH51) from the brown-rot fungus Gloeophyllum trabeum (GtAbf51A) was cloned and characterized in the present study. Analyses of the phylogeny of GH51 enzymes in wood rotting fungi revealed the existence of two groups, intercellular and extracellular enzymes. After deglycosylation, the recombinant GtAbf51A produced by Pichia pastoris appeared on SDS-PAGE as approximately 71,777 daltons, which is the expected molecular weight based on the amino acid sequence of GtAbf51A. Maximum enzyme activity occurred between pH 2.2 and 4.0 and at 50 °C, while it was stable between pH 2.2 and 10.0 and up to 40 °C. Due to the presence of a signal peptide, GtAbf51A was thought to hydrolyze polysaccharide containing arabinose. However, the hydrolysis rate of arabinosyl linkages in polysaccharides was only 3-5 % for arabinoxylan and 18 % for arabinan. GtAbf51A, in contrast, efficiently hydrolyzed arabinoxylooligosaccharides, particularly O-α-L-arabinofuranosyl-(1→3)-O-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose, which is the principal product of GH10 β-xylanase. These data suggest that GtAbf51A cooperates with other xylan-degrading enzymes, such as β-xylanase, to degrade xylan in nature.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/a0/08/70_jag.JAG-2022_0009.PMC10074032.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9272439","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}

引用次数: 0

In Vivo Digestibility of Carbohydrate Rich in Isomaltomegalosaccharide Produced from Starch by Dextrin Dextranase. 糊精葡聚糖酶从淀粉中提取的富含异麦芽糖的碳水化合物的体内消化率。

IF 1.1

Journal of applied glycoscience Pub Date : 2022-08-22 eCollection Date: 2022-01-01 DOI: 10.5458/jag.jag.JAG-2021_0013

Eri Kokubo, Hirofumi Sonoki, Kenta Aizawa, Hiroki Takagi, Masayasu Takada, Ayako Ito, Yuki Nakazato, Yasuhiro Takeda, Kazuhiro Miyaji

{"title":"In Vivo Digestibility of Carbohydrate Rich in Isomaltomegalosaccharide Produced from Starch by Dextrin Dextranase.","authors":"Eri Kokubo, Hirofumi Sonoki, Kenta Aizawa, Hiroki Takagi, Masayasu Takada, Ayako Ito, Yuki Nakazato, Yasuhiro Takeda, Kazuhiro Miyaji","doi":"10.5458/jag.jag.JAG-2021_0013","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2021_0013","url":null,"abstract":"Slowly digestible carbohydrates are needed for nutritional support in diabetic patients with malnutrition. They are a good source of energy and have the advantage that their consumption produces a low postprandial peak in blood glucose levels because they are slowly and completely digested in the small intestine. A high-amount isomaltomegalosaccharide containing carbohydrate (H-IMS), made from starch by dextrin dextranase, is a mixture of glucose polymers which has a continuous linear structure of α-1,6-glucosidic bonds and a small number of α-1,4-glucosidic bonds at the reducing ends. It has a broad degree of polymerization (DP) distribution with glucans of DP 10－30 as the major component. In our previous study, H-IMS has been shown to exhibit slow digestibility in vitro and not to raise postprandial blood glucose to such levels as that raised by dextrin in vivo. This marks it out as a potentially useful slowly digestible carbohydrate, and this study aimed to evaluate its in vivo digestibility. The amount of breath hydrogen emitted following oral administration of H-IMS was measured to determine whether any indigestible fraction passed through to and was fermented in the large intestine. Total carbohydrate in the feces was also measured. H-IMS, like glucose and dextrin, did not result in breath hydrogen excretion. Carbohydrate excretion with dietary H-IMS was no different from that of glucose or water. These results show that the H-IMS is completely digested and absorbed in the small intestine, indicating its potential as a slowly digestible carbohydrate in the diet of diabetic patients.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2022-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/7d/dd/69_jag.JAG-2021_0013.PMC9534827.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40653287","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}

引用次数: 0

Characterization of a GH Family 43 β-Xylosidase Having a Novel Carbohydrate-binding Module from Paenibacillus xylaniclasticus Strain TW1. 具有新型碳水化合物结合模块的GH家族43 β-木糖苷酶的鉴定

IF 1.1

Journal of applied glycoscience Pub Date : 2022-08-22 eCollection Date: 2022-01-01 DOI: 10.5458/jag.jag.JAG-2022_0001

Daichi Ito, Emiri Nakano, Shuichi Karita, Midori Umekawa, Khanok Ratanakhanokchai, Chakrit Tachaapaikoon

{"title":"Characterization of a GH Family 43 β-Xylosidase Having a Novel Carbohydrate-binding Module from Paenibacillus xylaniclasticus Strain TW1.","authors":"Daichi Ito, Emiri Nakano, Shuichi Karita, Midori Umekawa, Khanok Ratanakhanokchai, Chakrit Tachaapaikoon","doi":"10.5458/jag.jag.JAG-2022_0001","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0001","url":null,"abstract":"Paenibacillus xylaniclasticus strain TW1, a gram-positive facultative anaerobic bacterium, was isolated as a xylanolytic microorganism from the wastes of a pineapple processing factory. A gene encoding one of its xylanolytic enzymes, a β-xylosidase, was cloned and sequenced. Sequence analysis revealed that this β-xylosidase, named PxXyl43A, was composed of a glycoside hydrolase (GH) family 43 subfamily 12 catalytic module and an unknown function module (UM). The full-length PxXyl43A (PxXyl43A) was heterologously expressed in Escherichia coli and purified. Recombinant PxXyl43A exhibited hydrolysis activity against both p-nitrophenyl-β-D-xylopyranoside (pNPX) and p-nitrophenyl-α-L-arabinofuranoside at specific activities of 250 and 310 mU/mg, respectively. The optimal reaction pH and temperature for pNPX hydrolysis were 7.1 and 54 ˚C, respectively. At pH 7.0 and 54 ˚C, the K m and k cat for pNPX were 1.2 mM and 2.8 ± 0.15 s-1, respectively. It was also discovered that the recombinant unknown function module of PxXyl43A (PxXyl43A-UM) could bind to insoluble xylans like birchwood xylan and oat spelt xylan, whereas it did not bind to cellulosic substrates such as ball-milled cellulose, carboxymethyl cellulose or lichenan. The PxXyl43A-UM's binding constant value K a for oat spelt xylan was 2.0 × 10-5 M-1. These results suggest that PxXyl43A possesses a novel carbohydrate-binding module, named as CBM91, specific for xylan-containing polysaccharides.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2022-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/58/e0/69_jag.JAG-2022_0001.PMC9534826.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40444758","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}

引用次数: 1

GH-16 Type β-1,3-Glucanase from Lysobacter sp. MK9-1 Enhances Antifungal Activity of GH-19 Type Chitinase, and Its Glucan-binding Domain Binds to Fungal Cell-wall. 溶杆菌MK9-1中GH-16型β-1,3-葡聚糖酶增强了GH-19型几丁质酶的抗真菌活性，其葡聚糖结合结构域与真菌细胞壁结合。

IF 1.1

Journal of applied glycoscience Pub Date : 2022-08-22 eCollection Date: 2022-01-01 DOI: 10.5458/jag.jag.JAG-2022_0002

Yuitsu Otsuka, Koki Sato, Shigekazu Yano, Haruki Kanno, Wasana Suyotha, Hiroyuki Konno, Koki Makabe, Toki Taira

{"title":"GH-16 Type β-1,3-Glucanase from Lysobacter sp. MK9-1 Enhances Antifungal Activity of GH-19 Type Chitinase, and Its Glucan-binding Domain Binds to Fungal Cell-wall.","authors":"Yuitsu Otsuka, Koki Sato, Shigekazu Yano, Haruki Kanno, Wasana Suyotha, Hiroyuki Konno, Koki Makabe, Toki Taira","doi":"10.5458/jag.jag.JAG-2022_0002","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0002","url":null,"abstract":"The GH-16 type β-1,3-glucanase (BgluC16MK) gene of Lysobacter sp. MK9-1 was cloned to study its antifungal activities. BgluC16MK displays amino acid sequence similarity with GluC from L. enzymogenes strain N4-7. BgluC16MK includes a signal sequence, a catalytic domain and carbohydrate-binding module family 6-type β-glucan binding domain (B-GBD). The expression of the BgluC16MK gene in Escherichia coli without the signal sequence resulted in antifungal activity at a dose of 0.6-0.8 nmol/disk. However, BgluC16MK displayed antifungal activity at a dose of 0.025 nmol/disk in combination with Chi19MK. Substrate-specific assay revealed that purified BgluC16MK hydrolyzed insoluble curdlan more readily than the soluble substrate. Furthermore, to explore the binding selectivity of B-GBD of BgluC16MK, we constructed a fusion protein (B-GBD-GFP) using the B-GBD and green fluorescent protein. The activity of the fusion protein against various substrates indicates that B-GBD was selective for glucans with β-1,3-linkages. An additional study demonstrated the binding ability of B-GBD-GFP to the cell-wall of living fungi, such as T. reesei and Aspergillus oryzae. These findings suggest that BgluC16MK can be utilized to generate antifungal enzyme preparations and that the fusion protein B-GBD-GFP can be used to identify the fungal cell surface structure using β-glucans.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2022-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/9a/cf/69_jag.JAG-2022_0002.PMC9534828.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40651880","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}

引用次数: 1