Carbohydrate Research最新文献

{"title":"Characterization and engineering of Drosophila melanogaster β1-3-galactosyltransferase for glycoengineering applications","authors":"Linhan Wang ,&nbsp;Jichao Wei ,&nbsp;Fang Yuan ,&nbsp;Yongheng Rong ,&nbsp;Wanqian Du ,&nbsp;Wenjing Shi ,&nbsp;Xintan Wang ,&nbsp;Mei Wang ,&nbsp;Yankang Wang ,&nbsp;Anran Liu ,&nbsp;Junqiao Zhao ,&nbsp;Yun Kong ,&nbsp;Na Sun ,&nbsp;Wenzhu Tang ,&nbsp;Shengjun Wang","doi":"10.1016/j.carres.2025.109791","DOIUrl":"10.1016/j.carres.2025.109791","url":null,"abstract":"<div><div>β1-3-Galactosyltransferase from <em>Drosophila melanogaster</em> (<em>Dm</em>C1GalT1) plays a key role in O-glycan synthesis and holds considerable potential for glycoengineering applications. In this study, we achieved high-yield expression and purification of <em>Dm</em>C1GalT1 in <em>Escherichia coli,</em> obtaining over 5 mg of protein per liter of culture. Similar with the enzyme expressed from <em>Pichia pastoris</em>, this enzyme exhibited strict donor specificity towards UDP-Gal and efficiently galactosylated human CD74-derived Tn-glycopeptides. Structural analysis identified key residues involved in substrate binding and catalysis. Site-directed mutagenesis of active-site residues yielded variants with altered activity and stability profiles. Notably, the N108G and Y325W mutants retained high activity towards UDP-Gal but lost the ability to utilize UDP-GalNH₂, while N108A mutants retained 61.77 % of its activity toward UDP-Gal but maintained similar activity levels towards UDP-GalNH₂, while gaining weak but detectable activity toward UDP-Glc. These findings highlight the critical roles of residues N108 and Y325 in donor recognition. Thermal stability predictions using ProStab indicated that certain mutations affected enzyme stability without compromising activity. This work establishes an efficient platform for the expression, characterization, and engineering of <em>Dm</em>C1GalT1, facilitating the development of glycosyltransferase variants with tailored properties for synthetic glycobiology.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109791"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145755350","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Visible-light-promoted O-glycosylation with indolylthio glycosides","authors":"Tianyu Zhang ,&nbsp;Zefei Fan ,&nbsp;Yongyan Fu ,&nbsp;Yafei Hou ,&nbsp;Guanghui Ni","doi":"10.1016/j.carres.2025.109766","DOIUrl":"10.1016/j.carres.2025.109766","url":null,"abstract":"<div><div>A novel method for the preparation of thioglycoside donors from <span>d</span>-glucose and 2-indolone was developed. This method is straightforward to operate and enables highly efficient catalysis under mild conditions. In addition, a method for O-glycosylation of thioglycosides with various alcohols using trifluoromethyl thianthrenium triflate (TT-CF₃⁺TfO⁻) as an initiator and a visible light-induced photoredox catalysis method was also developed. The method is green, mild, easy to perform and does not require a neutralization step.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109766"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145617007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural characterization and immunomodulatory activity of a glucuronoarabinogalactooligosaccharide-complex pectin from the fruits of Aralia elata (Miq.) Seem","authors":"Tian-Yuan Wu ,&nbsp;Yong-Xin Huang ,&nbsp;Xu Liu ,&nbsp;Yu Shen ,&nbsp;Jun Liang ,&nbsp;Hai-Xue Kuang ,&nbsp;Yong-Gang Xia","doi":"10.1016/j.carres.2025.109763","DOIUrl":"10.1016/j.carres.2025.109763","url":null,"abstract":"<div><div>A novel glucuronoarabinogalactooligosaccharide-complex pectin, designated as <strong>AEFP-B₁</strong> (molecular weight: 7.352 × 10⁴ g/mol), was isolated from the fruits of <em>Aralia elata</em> using multiple chromatographic techniques. Its chemical structure was characterized by UPLC-ESI⁺-MS, GC–MS, HILIC-ESI^--HCD-MS, and 1/2D-NMR spectroscopy. The structural features of <strong>AEFP-B₁</strong> are as follows: (i) its backbone consists of homogalacturonan (HG) and rhamnogalacturonan-I (RG-I) regions at a molar ratio of 3:2; (ii) complex side chains, i.e., arabinogalactooligosaccharide, glucuronoarabinogalactooligosaccharide, glucuronogalactooligosaccharide and arabinan, are attached to the <em>C</em>-4 positions of rhamnosyl residues in the RG-I domain; (iii) a repetitive structural fragment was deduced, including →2)-Rha<em>p</em>-(1→, →2,4)-Rha<em>p</em>-(1→, Gal<em>p</em>A-(1→, →4)-Gal<em>p</em>A-(1→, →4)<em>-</em>Gal<em>p</em>A-6-OMe-(1→, Ara<em>f</em>-(1→, →3)-Ara<em>f</em>-(1→, →5)-Ara<em>f</em>-(1→, →3,5)-Ara<em>f</em>-(1→, Gal<em>p</em>-(1→, →3)-Gal<em>p</em>-1→, →4)-Gal<em>p</em>-(1→, →6)-Gal<em>p</em>-(1→, → 3,4)-Gal<em>p</em>-(1→, →3,4,6)-Gal<em>p</em>-(1→, and Glc<em>p</em>A-4-OMe-(1 → . Bioactivity assays demonstrated that <strong>AEFP-B₁</strong> could promote cytokine secretion and regulate immune responses. Surface plasmon resonance (SPR) analysis revealed that <strong>AEFP-B₁</strong> binds to toll-like receptor 2 (TLR2, dissociation constant <em>K</em>_D = 8.99 × 10⁻⁶ M) and toll-like receptor 4 (TLR4, <em>K</em>_D = 1.07 × 10⁻⁵ M), and this binding was further validated by molecular docking. To the best of our knowledge, this study is the first to isolate and structurally characterize pectic polysaccharides with immunomodulatory activity from <em>A. elata</em> fruits. It highlights the potential of <strong>AEFP-B₁</strong> for future applications both food and pharmaceutical industries.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109763"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145610606","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Site-selective CE4 enzyme from Rhodothermus marinus and diversified LmbE-Like catalysis in Bacillus cereus","authors":"Jun Bian,&nbsp;Pai Zang,&nbsp;Ran Tang,&nbsp;Can Wei,&nbsp;Yaqing Wang,&nbsp;Li Liu,&nbsp;Josef Voglmeir","doi":"10.1016/j.carres.2025.109792","DOIUrl":"10.1016/j.carres.2025.109792","url":null,"abstract":"<div><div>Chitooligosaccharides (COS) display diverse biological functions that depend strongly on their N-acetylation pattern, motivating enzymatic approaches that enable regioselective deacetylation. Here, we identified a CE4 deacetylase, RmCBDA2510 from <em>Rhodothermus marinus</em> that performs strict, site-selective, and chain-length-dependent mono-deacetylation of COS. Exoglycosidase probing together with MALDI-TOF/TOF MS/MS showed that RmCBDA2510 precisely generates AD (GlcNAc-GlcN), ADA (GlcNAc-GlcN-GlcNAc), and AADA (GlcNAc-GlcNAc-GlcN-GlcNAc) from chitobiose, chitotriose, and chitotetraose, respectively, revealing a distinctive internal subsite preference. The enzyme is thermophilic and alkaline-active, and site-directed mutagenesis identified Asp41 as essential for catalysis, establishing RmCBDA2510 as a highly selective biocatalyst for producing structurally uniform, partially deacetylated COS.</div><div>In contrast, the LmbE-like enzyme BCLmbE1534 from <em>Bacillus cereus</em> catalyzes both the deacetylation of <em>N</em>-acetylglucosamine glycosides and acylation/<em>trans</em>-acylation with short-chain fatty acids and biotin. This represents the first demonstration of <em>trans</em>-acylation within the LmbE family and expands its catalytic repertoire beyond simple deacetylation. Together, RmCBDA2510 and BCLmbE1534 provide complementary enzymatic platforms for tailoring COS structures and diversifying amino-sugar derivatives, thereby broadening the synthetic utility of carbohydrate-active deacetylases.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109792"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145773728","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Petasis-mediated exo-iminoglycals synthesis from glyconolactams allows access to unprecedented 1-spirocyclopropyl deoxynojirimycin","authors":"Lilou Chopin ,&nbsp;Aurélien Beato ,&nbsp;Dylan Yorga ,&nbsp;Nicolas Auberger ,&nbsp;Jean-Bernard Behr ,&nbsp;Jérôme Désiré ,&nbsp;Yves Blériot","doi":"10.1016/j.carres.2025.109765","DOIUrl":"10.1016/j.carres.2025.109765","url":null,"abstract":"<div><div>We report herein the olefination of a set of six <em>N</em>-Boc glyconolactams using Petasis reagent to yield unprecedented exoiminoglycals. In addition, a modified Simmons-Smith cyclopropanation was successfully applied to the D-<em>gluco</em>-configured olefin to furnish the unprecedented 1-spirocyclic deoxynojirimycin which proved to be a poor inhibitor of glycosidases in its unprotected form.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109765"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145733698","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biochemical and functional analysis of a thermostable, xylose-tolerant glycoside hydrolase 43 β-xylosidase from Thermothelomyces thermophilus","authors":"Ravi Kumar ,&nbsp;Shilpa Sharma ,&nbsp;Tulasi Satyanarayana","doi":"10.1016/j.carres.2025.109789","DOIUrl":"10.1016/j.carres.2025.109789","url":null,"abstract":"<div><div>The catalytic degradation of hemicellulose, particularly xylan, is critical for converting lignocellulosic biomass into economically valuable monosaccharides like xylose. β-xylosidases play a key role in this process by enabling efficient breakdown of xylan. Herein, a novel thermostable, xylose tolerant β-xylosidase from <em>Thermothelomyces thermophilus</em> (TtGH43) was codon-optimized, cloned and heterologously expressed in <em>Escherichia coli</em> BL21 (DE3), for the first time. Sequence analysis classified the enzyme as glycoside hydrolase 43 (GH43), sharing homology with fungal and bacterial GH43 β-xylosidases. Structural modelling confirmed the presence of conserved catalytic residues (glutamic and aspartic acid) critical for substrate binding and hydrolysis. Biochemical characterization revealed optimal activity of recombinant enzyme at 60 °C and pH 6.0, with robust stability under alkaline conditions. TtGH43 exhibited β-xylosidase activity towards synthetic substrates (e.g., <em>p</em>-nitrophenyl-β-<span>d</span>-xylopyranoside) as well as ability to degrade natural xylo-oligosaccharides. The enzyme demonstrated xylose tolerance up to 750 mM and retained activity in the presence of various metal ions and chemical additives. Additionally, TtGH43 maintained functionality under high-salt conditions, a rare-trait among fungal β-xylosidases. Overall, this study highlights TtGH43 as a promising enzyme candidate for industrial processes that demand alkali-tolerant and thermostable enzymes for efficient lignocellulosic biomass degradation.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109789"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145767251","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative evaluation of DNS, PAHBAH, and BCA colourimetric assays for quantifying reducing sugars","authors":"Lisa Coddens,&nbsp;Charlotte F. De Schepper,&nbsp;Kristof Brijs,&nbsp;Christophe M. Courtin","doi":"10.1016/j.carres.2025.109770","DOIUrl":"10.1016/j.carres.2025.109770","url":null,"abstract":"<div><div>Colourimetric assays for quantifying reducing sugars are widely used, including for assessing glycoside hydrolase activities. Consequently, there is a need for reliable high-throughput methodologies. Several protocols have been described in literature, with the most commonly used being the dinitrosalicylic acid (DNS), bicinchoninic acid (BCA) and <em>p</em>-hydroxybenzoic acid hydrazide (PAHBAH) assays. This study presents a comparative evaluation of these assays. Our results show that both the DNS and PAHBAH assays overestimate reducing sugar concentrations mainly due to saccharide degradation under alkaline conditions (pH ≥ 12.9) and high temperatures (100 °C) during the assays. To evaluate the impact of this overestimation, we experimentally measured glycoside hydrolase activity. All three assays overestimated reducing sugar concentrations compared to a reference method, though to varying extents. The BCA assay exhibited the least overestimation, likely due to minimal saccharide degradation under its milder alkaline conditions. It was therefore the most reliable method among those tested.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109770"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145660455","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evaluation of double-modified taro starch for the encapsulation and protection of bioactive compounds in Hibiscus Sabdariffa extract","authors":"Arely Bautista Rodríguez ,&nbsp;Apolonio Vargas-Torres ,&nbsp;Sylvia Rosales Chimal ,&nbsp;Ricardo O. Navarro Cortez ,&nbsp;Beatriz del Carmen Coutiño Laguna ,&nbsp;Heidi M. Palma-Rodríguez","doi":"10.1016/j.carres.2025.109768","DOIUrl":"10.1016/j.carres.2025.109768","url":null,"abstract":"<div><div>Taro starch was modified by ultrasound, enzymes, and a combination of both to evaluate structural changes and its performance as a wall material for encapsulation of <em>Hibiscus sabdariffa</em> extract. The double-modified starch (DMS) exhibited the lowest amylose content (6.7 %) and particle size (2.5 μm), in comparison with the native taro starch, which had 9.3 % and 3.3 μm, respectively. Pasting properties showed a 42 % decrease in peak viscosity of DMS relative to native starch, improving the efficiency of spray-drying. Stability studies showed that dual modification encapsulation (DME) retained 82 % of total phenolic compounds and 79 % of anthocyanins after seven days of storage under aging conditions. However, the retention decreased to 55 % and 48 %, respectively, after 35 days of storage. In the <em>in vitro</em> digestion model, ultrasound modification encapsulation (UME) showed the highest anthocyanin release (63 % gastric phase, 41 % intestinal phase), indicating gradual and controlled delivery. These findings indicate the potential of modified taro starch treatments to enhance the protection of bioactive drugs and provide greater control over the rate of compound release during the digestive process. These benefits are achieved while maintaining the stability and efficacy of the encapsulated compound.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109768"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145647415","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biopolymer electrolytes and composites based on chitosan for electrochemical processes: developing technologies, device integration, and ion transport mechanisms","authors":"Mesut Yılmazoğlu ,&nbsp;Tarek Kouka ,&nbsp;İlkay Güzel ,&nbsp;Ozan Coban ,&nbsp;Hikmet Okkay ,&nbsp;Noureddine El Messaoudi ,&nbsp;Mouslim Messali","doi":"10.1016/j.carres.2025.109778","DOIUrl":"10.1016/j.carres.2025.109778","url":null,"abstract":"<div><div>Chitosan, a biopolymer with multifunctionality that occurs naturally from chitin, was found to be an efficacious high-potential platform for building green polymer electrolytes and electrochemical device composite materials. Its inherent properties like dense functional groups, biocompatibility, film-forming nature, and ease of chemical modification, favorably position it as a reliable substitute for conventional synthetic polymers. This review encompasses chitosan-based biopolymer electrolytes and composites, the mechanism of ionic conductance, structural tuning, and their incorporation into high-performance electrochemical devices. The review places particular importance on recent strategies pursued for enhancing ionic conductivity, mechanical stability, and electrochemical performance by chemical functionalization, blending, and nanomaterial inclusion. Particular focus is placed on ion dynamic awareness, proton and cation conducting channels, and polymer–filler interaction for charge transportation optimization. Application domains of fuel cell, battery, supercapacitor, and bioelectronic devices are comprehensively discussed with focus placed on both the achievements and ongoing challenges of chitosan systems. Finally, the review challenges issues of durability, scalability, and sustainability and outlines directions for future material engineering and technology integration. Bridging the gap between fundamental knowledge and real-world applications, this review article serves to illustrate the potential of chitosan-based electrolytes and composites to propel next-generation green and high-performance electrochemical technologies.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109778"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145616999","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A structurally defined galactoglucan from Arisaema erubescens with a multi-target tumor-associated protein binding domain","authors":"Yue Zhu ,&nbsp;Can Jin ,&nbsp;Kan Ding","doi":"10.1016/j.carres.2025.109781","DOIUrl":"10.1016/j.carres.2025.109781","url":null,"abstract":"<div><div>As targeted therapy assumes an increasingly pivotal role in comprehensive cancer treatment, there is a growing imperative to develop natural drugs that exhibit low toxicity and minimal side effects. Polysaccharides derived from the traditional Chinese herbal medicine <em>Arisaema erubescens</em> have been reported to show antitumor potential, however the key structural features and specific molecular targets responsible for their pharmacological effects are still vague. To address this question, a homogeneous polysaccharide TNX05 (<em>Mw</em> ≈ 9 kDa) was obtained and characterized from <em>Arisaema erubescens</em>. Structural analysis suggested that TNX05 was a galactoglucan with a backbone of 1, 4-α-_D-Glc<em>p</em>, 1, 4-β-_D-Glc<em>p</em>, and 1, 3-β-_D-Gal<em>p</em> residues, with side chains—→1-α/β-_D-Glc<em>p</em>-(6 → 1)-α-_D-Glc<em>p</em> and →1)-α-_D-Glc<em>p</em>—substituted at the C-4 and C-6 of the 1, 4-α-_D-Glc<em>p</em> units, respectively. Combining enzymatic hydrolysis, molecular docking, and protein-binding assays we showed a key core domain (TNX05II), which exhibited micromolar-range binding affinity for ten tumor-associated targets: Glypican-6 (GPC-6), glucuronic acid epimerase (Glce), S100 calcium-binding protein A4 (S100A4), S100A6, nucleoside diphosphate kinase 1 (NME1), fibroblast growth factor 17 (FGF17), proto-oncogene tyrosine-protein kinase Src (SRC), kelch-like ECH-associated protein 1 (KEAP1), Galectin-3 (Gal-3), and protein phosphatase 3 catalytic subunit alpha (PPP3CA). Additionally, TNX05II was significantly resistant to α-glucosidase degradation. This study suggests a possible key structure-target relationship underlying TNX05's antitumor activity, providing a molecular basis for the antitumor mechanism of Arisaema polysaccharides.</div></div>","PeriodicalId":9415,"journal":{"name":"Carbohydrate Research","volume":"560 ","pages":"Article 109781"},"PeriodicalIF":2.5,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145676638","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}