Journal of applied glycoscience最新文献

{"title":"Water Sorption Isotherm and Critical Water Activity of Amorphous Water-Soluble Carbohydrates Characterized by the Glass Transition Temperature.","authors":"Yuichi Kashiwakura, Tomochika Sogabe, Sukritta Anantawittayanon, Takumi Mochizuki, Kiyoshi Kawai","doi":"10.5458/jag.jag.JAG-2023_0015","DOIUrl":"10.5458/jag.jag.JAG-2023_0015","url":null,"abstract":"<p><p>Water-soluble carbohydrates commonly exist in an amorphous state in foods and undergo glass-rubber transition (glass transition) at the glass transition temperature (<i>T</i>_g). The critical water content (<i>W</i>_c) and critical water activity (<i>a</i>_wc) are the water content and water activity (<i>a</i>_w) at which the glass transition occurs at 298 K (typical ambient temperature), respectively. For amorphous water-soluble carbohydrates, <i>W</i>_c can be predicted from the <i>T</i>_g of anhydrous solid (<i>T</i>_gs) using previously reported equations. However, an approach for predicting <i>a</i>_wc is still lacking. This study aimed to establish an <i>a</i>_wc-predictive approach for amorphous water-soluble carbohydrates based on <i>T</i>_gs. First, the water sorption isotherms of four hydrogenated starch hydrolysates were investigated, and the results were analyzed using the Guggenheim-Anderson-de Boer (GAB) model. Second, the effect of <i>T</i>_gs on the GAB parameters (<i>C</i>, <i>K</i>, and <i>W</i>_m) was evaluated using the <i>T</i>_gs values reported in previous literatures. <i>C</i> and <i>W</i>_m decreased and increased logarithmically, respectively, with increasing 1/<i>T</i>_gs. <i>K</i> was fixed to 1 (constant), as it showed little variation. These results enabled the prediction of the GAB parameters from <i>T</i>_gs. The GAB model could then predict <i>a</i>_wc from <i>W</i>_c, which was determined using the previously established equations. The predicted <i>a</i>_wc values were in good agreement with the experimentally determined <i>a</i>_wc. Additionally, we demonstrated that this <i>a</i>_wc-prediction approach is also applicable to amorphous water-soluble electrolytes and partially water-insoluble carbohydrates. Thus, this approach can be used for the quality control of amorphous water-soluble carbohydrates and carbohydrate-based foods.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 1","pages":"15-21"},"PeriodicalIF":1.1,"publicationDate":"2024-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11117189/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141154924","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":"Promotion of Thermal Inactivation Treatment of Apple Polyphenol Oxidase in the Presence of Trehalose.","authors":"Shinya Yamazaki, Ibuki Shirata, Masahiro Mizuno, Yoshihiko Amano","doi":"10.5458/jag.jag.JAG-2023_0009","DOIUrl":"10.5458/jag.jag.JAG-2023_0009","url":null,"abstract":"<p><p>Trehalose is known to protect enzymes from denaturation. In the present study, we observed promotion of apple polyphenol oxidase (PPO) inactivation in a trehalose solution with thermal treatment. Crude PPO from Fuji apple was mixed with either sucrose or trehalose solutions, then the samples treated at 25 or 65 °C. In the presence of trehalose, PPO activities were markedly decreased upon treatment at 65 °C with increasing trehalose concentration. Furthermore, the reduction in PPO activity in the presence of trehalose was proportional to storage time after thermal treatment and thermal treatment time. Comparing PPO activities between treatment time 0 and 90 min at 65 °C, activities decreased 89 % for trehalose concentration of 0.2 M. These results indicates that trehalose acts not only as inhibitor but as promoter of inactivation of PPO. The Lineweaver-Burk plot indicated that trehalose acts on PPO as a non-competitive inhibitor during the 65 °C treatment. Two mechanisms of PPO inactivation in the presence of trehalose were suggested; one is the suppression of PPO activation cause by a thermal treatment, and another is the conformational change to inactivation form of PPO in conjunction with trehalose and a thermal treatment. Additionally, apple juice including 0.2 or 0.5 M trehalose with 65 °C treatment indicated slow browning than the juice with 0.2 or 0.5 M sucrose or without sugars. This result demonstrates that the preventing of browning with trehalose is a viable industrial food process.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 1","pages":"1-7"},"PeriodicalIF":1.1,"publicationDate":"2024-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11116086/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141156174","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":"Purification and Characterization of α-Mannosidase from Onion, <i>Allium cepa</i>.","authors":"Yui Narita, Yota Tatara, Shigeki Hamada, Kaoru Kojima, Shuai Li, Takashi Yoshida","doi":"10.5458/jag.jag.JAG-2023_0010","DOIUrl":"10.5458/jag.jag.JAG-2023_0010","url":null,"abstract":"<p><p>α-Mannosidase (ALMAN) extracted from onion (<i>Allium cepa</i>) was purified by column chromatography such as hydrophobic and gel filtration. ALMAN is an acidic α-mannosidase that exhibits maximum activity against <i>p</i>NP-α-Man at pH 4.0-5.0 at 50°C. Amino acid sequence analysis of ALMAN was consistent with α-mannosidase deduced from <i>Allium cepa</i> transcriptome analysis. The gene <i>alman</i> was amplified by PCR using mRNA extracted from onions, and a full-length gene of 3,054 bp encoding a protein of 1,018 amino acid residues was revealed. ALMAN is classified as Glycoside Hydrolase Family (GH) 38 and showed homology with other plant-derived α-mannosidases such as tomato and hot pepper.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 1","pages":"33-36"},"PeriodicalIF":1.1,"publicationDate":"2024-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11116084/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141154922","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":"Identification and characterization of novel intracellular α-xylosidase in &lt;i&gt;Aspergillus oryzae&lt;/i&gt;","authors":"Tomohiko Matsuzawa, Yusuke Nakamichi, Naoki Shimada","doi":"10.5458/jag.jag.jag-2023_0007","DOIUrl":"https://doi.org/10.5458/jag.jag.jag-2023_0007","url":null,"abstract":"α-Xylosidase releases xylopyranosyl side chains from xyloglucan oligosaccharides and is vital for xyloglucan degradation. Previously, we identified and characterized two α-xylosidases, intracellular AxyA and extracellular AxyB, in Aspergillus oryzae. In this study, we identified a third α-xylosidase, termed AxyC, in A. oryzae. These three A. oryzae α-xylosidases belong to the glycoside hydrolase family 31, but there are clear differences in substrate specificity. Both AxyA and AxyB showed much higher hydrolytic activity toward isoprimeverose (α-D-xylopyranosyl-1,6-glucose) than p-nitrophenyl α-D-xylopyranoside. In contrast, the specific activity of AxyC toward the p-nitrophenyl substrate was approximately 950-fold higher than that toward isoprimeverose. Our study revealed that there are multiple α-xylosidases with different substrate specificities in A. oryzae.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"38 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135098727","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A C1/C4-Oxidizing AA10 Lytic Polysaccharide Monooxygenase from <i>Paenibacillus xylaniclasticus</i> Strain TW1.","authors":"Daichi Ito,&nbsp;Shuichi Karita,&nbsp;Midori Umekawa","doi":"10.5458/jag.jag.JAG-2022_0011","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0011","url":null,"abstract":"<p><p>Lytic polysaccharide monooxygenases (LPMO) are key enzymes for the efficient degradation of lignocellulose biomass with cellulases. A lignocellulose-degradative strain, <i>Paenibacillus xylaniclasticus</i> TW1, has LPMO-encoding <i>Px</i>AA10A gene. Neither the C1/C4-oxidizing selectivity nor the enzyme activity of <i>Px</i>AA10A has ever been characterized. In this study, the C1/C4-oxidizing selectivity of <i>Px</i>AA10A and the boosting effect for cellulose degradation with a cellulase cocktail were investigated. The full-length <i>Px</i>AA10A (r<i>Px</i>AA10A) and the catalytic domain (r<i>Px</i>AA10A-CD) were heterologously expressed in <i>Escherichia coli</i> and purified. To identify the C1/C4-oxidizing selectivity of <i>Px</i>AA10A, cellohexaose was used as a substrate with the use of r<i>Px</i>AA10A-CD, and the products were analyzed by MALDI-TOF/MS. As a result, aldonic acid cellotetraose and cellotetraose, the products from C1-oxidization and C4-oxidization, respectively, were detected. These results indicate that <i>Px</i>AA10A is a C1/C4-oxidizing LPMO. It was also found that the addition of r<i>Px</i>AA10A into a cellulase cocktail enhanced the cellulose-degradation efficiency.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 1","pages":"39-42"},"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/a3/4f/70_jag.JAG-2022_0011.PMC10074029.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9272436","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":"Identification and Characterization of Dextran α-1,2-Debranching Enzyme from <i>Microbacterium dextranolyticum</i>.","authors":"Takatsugu Miyazaki,&nbsp;Hidekazu Tanaka,&nbsp;Shuntaro Nakamura,&nbsp;Hideo Dohra,&nbsp;Kazumi Funane","doi":"10.5458/jag.jag.JAG-2022_0013","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0013","url":null,"abstract":"<p><p>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 <i>Leuconostoc</i> bacteria. DDE was isolated from <i>Microbacterium dextranolyticum</i> (formerly known as <i>Flavobacterium</i> 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 <i>Arthrobacter globiformis</i> glucodextranase, and a transmembrane region at the C-terminus. Recombinant DDE released glucose from α-(1→2)-branched α-glucans produced by <i>Leuconostoc citreum</i> 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 <i>Leuconostoc citreum</i> 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.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 1","pages":"15-24"},"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}

{"title":"Function and Structure of <i>Lacticaseibacillus casei</i> GH35 β-Galactosidase LBCZ_0230 with High Hydrolytic Activity to Lacto-<i>N</i>-biose I and Galacto-<i>N</i>-biose.","authors":"Wataru Saburi,&nbsp;Tomoya Ota,&nbsp;Koji Kato,&nbsp;Takayoshi Tagami,&nbsp;Keitaro Yamashita,&nbsp;Min Yao,&nbsp;Haruhide Mori","doi":"10.5458/jag.jag.JAG-2022_0014","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0014","url":null,"abstract":"<p><p>β-Galactosidase (EC 3.2.1.23) hydrolyzes β-D-galactosidic linkages at the non-reducing end of substrates to produce β-D-galactose. <i>Lacticaseibacillus casei</i> 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-<i>N</i>-biose I (LNB; Galβ1-3GlcNAc) and galacto-<i>N</i>-biose (GNB; Galβ1-3GalNAc) <i>via</i> the phosphoenolpyruvate: sugar phosphotransferase system. The GH35 protein (GnbG) from <i>L. casei</i> 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, <i>L. casei</i> JCM1134 LBCZ_0230, homologous to GnbG, was characterized enzymatically and structurally. A recombinant LBCZ_0230, produced in <i>Escherichia coli</i>, exhibited high hydrolytic activity toward <i>o</i>-nitrophenyl β-D-galactopyranoside, <i>p</i>-nitrophenyl β-D-galactopyranoside, LNB, and GNB, but not toward <i>o</i>-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 <i>Streptococcus pneumoniae</i> 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 <i>N</i>-acetyl-D-glucosamine residue of LNB at subsite +1.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 2","pages":"43-52"},"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}

{"title":"Effect of Water Vapor Sorption on Complex Formation in Amylose-lauric Acid Blend Powder.","authors":"Yuki Yoshitomi,&nbsp;Kiyoshi Kawai","doi":"10.5458/jag.jag.JAG-2023_0001","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2023_0001","url":null,"abstract":"<p><p>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 (∆<i>H</i>_m) 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 ∆<i>H</i>_m 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 ∆<i>H</i>_m 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 %.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 2","pages":"53-58"},"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}

{"title":"Molecular Weight Distribution of Whole Starch in Rice Endosperm by Gel-permeation Chromatography.","authors":"Naoto Suzuki,&nbsp;Isao Hanashiro,&nbsp;Naoko Fujita","doi":"10.5458/jag.jag.JAG-2022_0010","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0010","url":null,"abstract":"<p><p>Starch is comprised of very large α-glucan molecules composed primarily of linear amylose and highly branched amylopectin. Most methods for analyses of starch structure use hydrolytic enzymes to cleave starch. When undegraded, whole starch structures can be analyzed by gel-permeation chromatography (GPC), but this typically yields a single peak each for amylopectin and amylose. The objective of this study was to stably separate amylopectins in whole starch based on their molecular weight using GPC, and to determine the structure of each peak. When alkali-gelatinized whole starch was applied to GPC columns (Toyopearl HW75S × 2, HW65S, and HW55S), it was separated into three peaks. Iodine staining and chain length distribution analyses of debranched samples showed that peaks were mainly composed of high-molecular weight (MW) amylopectin consisting of many clusters, low-MW amylopectin consisting of a small number of clusters, and amylose.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 1","pages":"25-32"},"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/ed/2f/70_jag.JAG-2022_0010.PMC10074033.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9272437","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":"Automatic Calculation of the Kinetic Parameters of Enzymatic Reactions with Their Standard Errors Using Microsoft Excel.","authors":"Motomitsu Kitaoka","doi":"10.5458/jag.jag.JAG-2022_0012","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0012","url":null,"abstract":"<p><p>We created a Microsoft Excel file, Enzyme_Kinetics_Calculator, which includes macro programs that automatically calculates kinetic parameters for typical kinetic equations of enzymatic reactions, accompanied by their standard errors, by minimizing the residual sum of squares thereof. The [<i>S</i>]-<i>v</i> plot is automatically drawn with the theoretical lines and, similarly, the 1/[<i>S</i>]-1/<i>v</i> plot in the case of linear theoretical lines. Enzyme_Kinetics_Calculator is available as a supplementary file for this paper (see J. Appl. Glycosci. Web site).</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 1","pages":"33-37"},"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/b5/e7/70_jag.JAG-2022_0012.PMC10074026.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9273038","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}