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Pesquisa : D08.811.277.450.420.200.200 [Categoria DeCS]
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  1 / 5606 MEDLINE  
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[PMID]:29323888
[Au] Autor:Hosseini SH; Hosseini SA; Zohreh N; Yaghoubi M; Pourjavadi A
[Ad] Endereço:Department of Chemical Engineering, University of Science and Technology of Mazandaran , Behshahr, Iran.
[Ti] Título:Covalent Immobilization of Cellulase Using Magnetic Poly(ionic liquid) Support: Improvement of the Enzyme Activity and Stability.
[So] Source:J Agric Food Chem;66(4):789-798, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A magnetic nanocomposite was prepared by entrapment of Fe O nanoparticles into the cross-linked ionic liquid/epoxy type polymer. The resulting support was used for covalent immobilization of cellulase through the reaction with epoxy groups. The ionic surface of the support improved the adsorption of enzyme, and a large amount of enzyme (106.1 mg/g) was loaded onto the support surface. The effect of the presence of ionic monomer and covalent binding of enzyme was also investigated. The structure of support was characterized by various instruments such as FT-IR, TGA, VSM, XRD, TEM, SEM, and DLS. The activity and stability of immobilized cellulase were investigated in the prepared support. The results showed that the ionic surface and covalent binding of enzyme onto the support improved the activity, thermal stability, and reusability of cellulase compared to free cellulase.
[Mh] Termos MeSH primário: Celulase/química
Celulase/metabolismo
Enzimas Imobilizadas/química
Líquidos Iônicos
Fenômenos Magnéticos
Polímeros
[Mh] Termos MeSH secundário: Adsorção
Estabilidade Enzimática
Enzimas Imobilizadas/metabolismo
Compostos Férricos
Temperatura Alta
Nanopartículas de Magnetita/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Ferric Compounds); 0 (Ionic Liquids); 0 (Magnetite Nanoparticles); 0 (Polymers); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b03922


  2 / 5606 MEDLINE  
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[PMID]:29261692
[Au] Autor:Stempien E; Goddard ML; Wilhelm K; Tarnus C; Bertsch C; Chong J
[Ad] Endereço:Université de Haute-Alsace, Laboratoire Vigne, Biotechnologies et Environnement, Colmar, France.
[Ti] Título:Grapevine Botryosphaeria dieback fungi have specific aggressiveness factor repertory involved in wood decay and stilbene metabolization.
[So] Source:PLoS One;12(12):e0188766, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Grapevine trunk diseases: Eutypa dieback, esca and Botryosphaeria dieback, which incidence has increased recently, are associated with several symptoms finally leading to the plant death. In the absence of efficient treatments, these diseases are a major problem for the viticulture; however, the factors involved in disease progression are not still fully identified. In order to get a better understanding of Botryosphaeria dieback development in grapevine, we have investigated different factors involved in Botryosphaeriaceae fungi aggressiveness. We first evaluated the activity of the wood-degrading enzymes of different isolates of Neofusicoccum parvum and Diplodia seriata, two major fungi associated with Botryosphaeria dieback. We further examinated the ability of these fungi to metabolize major grapevine phytoalexins: resveratrol and δ-viniferin. Our results demonstrate that Botryosphaeriaceae were characterized by differential wood decay enzymatic activities and have the capacity to rapidly degrade stilbenes. N. parvum is able to degrade parietal polysaccharides, whereas D. seriata has a better capacity to degrade lignin. Growth of both fungi exhibited a low sensitivity to resveratrol, whereas δ-viniferin has a fungistatic effect, especially on N. parvum Bourgogne S-116. We further show that Botryosphaeriaceae are able to metabolize rapidly resveratrol and δ-viniferin. The best stilbene metabolizing activity was measured for D. seriata. In conclusion, the different Botryosphaeriaceae isolates are characterized by a specific aggressiveness repertory. Wood and phenolic compound decay enzymatic activities could enable Botryosphaeriaceae to bypass chemical and physical barriers of the grapevine plant. The specific signature of Botryosphaeriaceae aggressiveness factors could explain the importance of fungi complexes in synergistic activity in order to fully colonize the host.
[Mh] Termos MeSH primário: Ascomicetos/patogenicidade
Estilbenos/metabolismo
Vitis/microbiologia
Madeira
[Mh] Termos MeSH secundário: Ascomicetos/crescimento & desenvolvimento
Ascomicetos/metabolismo
Celulase/metabolismo
Polissacarídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polysaccharides); 0 (Stilbenes); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188766


  3 / 5606 MEDLINE  
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[PMID]:29253879
[Au] Autor:Chen J; Liu X; Li F; Li Y; Yuan D
[Ad] Endereço:Hainan Key Laboratory of Banana Genetic Improvement, Haikou Experimental Station, Chinese Academy of Tropical Agricultural Sciences, Haikou, China.
[Ti] Título:Cold shock treatment extends shelf life of naturally ripened or ethylene-ripened avocado fruits.
[So] Source:PLoS One;12(12):e0189991, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Avocado is an important tropical fruit with high commercial value, but has a relatively short storage life. In this study, the effects of cold shock treatment (CST) on shelf life of naturally ripened and ethylene-ripened avocado fruits were investigated. Fruits were immersed in ice water for 30 min, then subjected to natural or ethylene-induced ripening. Fruit color; firmness; respiration rate; ethylene production; and the activities of polygalacturonase (PG), pectin methylesterase (PME), and endo-ß-1,4-glucanase were measured. Immersion in ice water for 30 min effectively delayed ripening-associated processes, including peel discoloration, pulp softening, respiration rate, and ethylene production during shelf life. The delay in fruit softening by CST was associated with decreased PG and endo-ß-1,4-glucanase activities, but not PME activity. This method could potentially be a useful postharvest technology to extend shelf life of avocado fruits.
[Mh] Termos MeSH primário: Temperatura Baixa
Etilenos/farmacologia
Frutas
Persea
[Mh] Termos MeSH secundário: Hidrolases de Éster Carboxílico/química
Parede Celular
Celulase/química
Pectinas/química
Poligalacturonase/química
Fatores de Tempo
Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ethylenes); 0 (Pectins); 059QF0KO0R (Water); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.11 (pectinesterase); EC 3.2.1.15 (Polygalacturonase); EC 3.2.1.4 (Cellulase); EC 3.2.1.4 (endoglucanase EGL1)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189991


  4 / 5606 MEDLINE  
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[PMID]:29199828
[Au] Autor:Sun X; Xue X; Li M; Gao F; Hao Z; Huang H; Luo H; Qin L; Yao B; Su X
[Ad] Endereço:Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences , Beijing 100081, China.
[Ti] Título:Efficient Coproduction of Mannanase and Cellulase by the Transformation of a Codon-Optimized Endomannanase Gene from Aspergillus niger into Trichoderma reesei.
[So] Source:J Agric Food Chem;65(50):11046-11053, 2017 Dec 20.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellulase and mannanase are both important enzyme additives in animal feeds. Expressing the two enzymes simultaneously within one microbial host could potentially lead to cost reductions in the feeding of animals. For this purpose, we codon-optimized the Aspergillus niger Man5A gene to the codon-usage bias of Trichoderma reesei. By comparing the free energies and the local structures of the nucleotide sequences, one optimized sequence was finally selected and transformed into the T. reesei pyridine-auxotrophic strain TU-6. The codon-optimized gene was expressed to a higher level than the original one. Further expressing the codon-optimized gene in a mutated T. reesei strain through fed-batch cultivation resulted in coproduction of cellulase and mannanase up to 1376 U·mL and 1204 U·mL , respectively.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Celulase/genética
Códon/genética
Proteínas Fúngicas/genética
Trichoderma/genética
beta-Manosidase/genética
[Mh] Termos MeSH secundário: Aspergillus niger/genética
Celulase/química
Celulase/metabolismo
Celulose/metabolismo
Códon/metabolismo
Proteínas Fúngicas/metabolismo
Cinética
Engenharia de Proteínas
Trichoderma/metabolismo
beta-Manosidase/química
beta-Manosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (Fungal Proteins); 9004-34-6 (Cellulose); EC 3.2.1.25 (beta-Mannosidase); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180110
[Lr] Data última revisão:
180110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05114


  5 / 5606 MEDLINE  
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[PMID]:29180013
[Au] Autor:Kwon KK; Yeom SJ; Lee DH; Jeong KJ; Lee SG
[Ad] Endereço:Synthetic Biology and Bioengineering Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Republic of Korea; Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141, Republic of Korea
[Ti] Título:Development of a novel cellulase biosensor that detects crystalline cellulose hydrolysis using a transcriptional regulator.
[So] Source:Biochem Biophys Res Commun;495(1):1328-1334, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Successful utilization of cellulose as renewable biomass depends on the development of economically feasible technologies, which can aid in enzymatic hydrolysis. In this study, we developed a whole-cell biosensor for detecting cellulolytic activity that relies on the recognition of cellobiose using the transcriptional factor CelR from Thermobifida fusca and transcriptional activation of its downstream gfp reporter gene. The fluorescence intensity of whole-cell biosensor, which was named as cellobiose-detectible genetic enzyme screening system (CBGESS), was directly proportional to the concentration of cellobiose. The strong fluorescence intensity of CBGESS demonstrated the ability to detect cellulolytic activity with two cellulosic substrates, carboxymethyl cellulose and p-nitrophenyl ß-D-cellobioside in cellulase-expressing Escherichia coli. In addition, CBGESS easily sensed crystalline cellulolytic activity when commercial Celluclast 1.5L was dropped on an Avicel plate. Therefore, CBGESS is a powerful tool for detecting cellulolytic activity with high sensitivity in the presence of soluble or insoluble cellulosic substrates. CBGESS may be further applied to excavate novel cellulases or microbes from both genetic libraries and various environments.
[Mh] Termos MeSH primário: Bioensaio/métodos
Técnicas Biossensoriais/métodos
Celulase/metabolismo
Celulose/metabolismo
Escherichia coli/metabolismo
Espectrometria de Fluorescência/métodos
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Celulose/análise
Cristalização
Hidrólise
Técnicas de Sonda Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Transcription Factors); 9004-34-6 (Cellulose); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE


  6 / 5606 MEDLINE  
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[PMID]:28745859
[Au] Autor:Chaffey PK; Guan X; Wang X; Ruan Y; Li Y; Miller SG; Tran AH; Koelsch TN; Pass LF; Tan Z
[Ad] Endereço:Department of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado , Boulder, Colorado 80303, United States.
[Ti] Título:Quantitative Effects of O-Linked Glycans on Protein Folding.
[So] Source:Biochemistry;56(34):4539-4548, 2017 08 29.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein O-glycosylation is a diverse, common, and important post-translational modification of both proteins inside the cell and those that are secreted or membrane-bound. Much work has shown that O-glycosylation can alter the structure, function, and physical properties of the proteins to which it is attached. One gap remaining in our understanding of O-glycoproteins is how O-glycans might affect the folding of proteins. Here, we took advantage of synthetic, homogeneous O-glycopeptides to show that certain glycosylation patterns have an intrinsic effect, independent of any cellular folding machinery, on the folding pathway of a model O-glycoprotein, a carbohydrate binding module (CBM) derived from the Trichoderma reesei cellulase TrCel7A. The strongest effect, a 6-fold increase in overall folding rate, was observed when a single O-mannose was the glycan, and the glycosylation site was near the N-terminus of the peptide sequence. We were also able to show that glycosylation patterns affected the kinetics of each step in unique ways, which may help to explain the observations made here. This work is a first step toward quantitative understanding of how O-glycosylation might control, through intrinsic means, the folding of O-glycoproteins. Such an understanding is expected to facilitate future investigations into the effects of glycosylation on more biological processes related to protein folding.
[Mh] Termos MeSH primário: Celulase/metabolismo
Proteínas Fúngicas/metabolismo
Glicoproteínas/metabolismo
Polissacarídeos/metabolismo
Dobramento de Proteína
Trichoderma/enzimologia
[Mh] Termos MeSH secundário: Celulase/química
Celulase/genética
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Glicoproteínas/química
Glicoproteínas/genética
Polissacarídeos/química
Polissacarídeos/genética
Trichoderma/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Glycoproteins); 0 (Polysaccharides); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171206
[Lr] Data última revisão:
171206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00483


  7 / 5606 MEDLINE  
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[PMID]:29023528
[Au] Autor:Asem D; Leo VV; Passari AK; Tonsing MV; Joshi JB; Uthandi S; Hashem A; Abd Allah EF; Singh BP
[Ad] Endereço:Molecular Microbiology and Systematics Laboratory, Department of Biotechnology, Aizawl, Mizoram University, Mizoram, India.
[Ti] Título:Evaluation of gastrointestinal bacterial population for the production of holocellulose enzymes for biomass deconstruction.
[So] Source:PLoS One;12(10):e0186355, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The gastrointestinal (GI) habitat of ruminant and non-ruminant animals sustains a vast ensemble of microbes that are capable of utilizing lignocellulosic plant biomass. In this study, an indigenous swine (Zovawk) and a domesticated goat (Black Bengal) were investigated to isolate bacteria having plant biomass degrading enzymes. After screening and enzymatic quantification of eighty-one obtained bacterial isolates, Serratia rubidaea strain DBT4 and Aneurinibacillus aneurinilyticus strain DBT87 were revealed as the most potent strains, showing both cellulase and xylanase production. A biomass utilization study showed that submerged fermentation (SmF) of D2 (alkaline pretreated pulpy biomass) using strain DBT4 resulted in the most efficient biomass deconstruction with maximum xylanase (11.98 U/mL) and FPase (0.5 U/mL) activities (55°C, pH 8). The present study demonstrated that bacterial strains residing in the gastrointestinal region of non-ruminant swine are a promising source for lignocellulose degrading microorganisms that could be used for biomass conversion.
[Mh] Termos MeSH primário: Bacillales/enzimologia
Celulase/metabolismo
Trato Gastrointestinal/microbiologia
Serratia/enzimologia
[Mh] Termos MeSH secundário: Animais
Bacillales/classificação
Bacillales/genética
Bacillales/isolamento & purificação
Biomassa
Endo-1,4-beta-Xilanases/metabolismo
Cabras
Concentração de Íons de Hidrogênio
Cinética
Lignina/química
Lignina/metabolismo
Microscopia Eletrônica de Varredura
Filogenia
RNA Ribossômico 16S/classificação
RNA Ribossômico 16S/metabolismo
Serratia/classificação
Serratia/genética
Serratia/isolamento & purificação
Espectroscopia de Infravermelho com Transformada de Fourier
Suínos
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Ribosomal, 16S); 11132-73-3 (lignocellulose); 9005-53-2 (Lignin); EC 3.2.1.4 (Cellulase); EC 3.2.1.8 (Endo-1,4-beta Xylanases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171013
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186355


  8 / 5606 MEDLINE  
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[PMID]:28873985
[Au] Autor:Badino SF; Bathke JK; Sørensen TH; Windahl MS; Jensen K; Peters GHJ; Borch K; Westh P
[Ad] Endereço:Research Unit for Functional Biomaterials, Department of Science and Environment, INM, Roskilde University, 1 Universitetsvej, Build. 28 C, DK-4000, Roskilde, Denmark.
[Ti] Título:The influence of different linker modifications on the catalytic activity and cellulose affinity of cellobiohydrolase Cel7A from Hypocrea jecorina.
[So] Source:Protein Eng Des Sel;30(7):495-501, 2017 Jul 01.
[Is] ISSN:1741-0134
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Various cellulases consist of a catalytic domain connected to a carbohydrate-binding module (CBM) by a flexible linker peptide. The linker if often strongly O-glycosylated and typically has a length of 20-50 amino acid residues. Functional roles, other than connecting the two folded domains, of the linker and its glycans, have been widely discussed, but experimental evidence remains sparse. One of the most studied cellulose degrading enzymes is the multi-domain cellobiohydrolase Cel7A from Hypocrea jecorina. Here, we designed variants of Cel7A with mutations in the linker region to elucidate the role of the linker. We found that moderate modification of the linker could result in significant changes in substrate affinity and catalytic efficacy. These changes were quite different for different linker variants. Thus, deletion of six residues near the catalytic domain had essentially no effects on enzyme function. Conversely, a substitution of four glycosylation sites near the middle of the linker reduced substrate affinity and increased maximal turnover. The observation of weaker binding provides some support of recent suggestions that linker glycans may be directly involved in substrate interactions. However, a variant with several inserted glycosylation sites near the CBM also showed lower affinity for the substrate compared to the wild-type, and we suggest that substrate interactions of the glycans depend on their exact location as well as other factors such as changes in structure and dynamics of the linker peptide.
[Mh] Termos MeSH primário: Catálise
Celulose 1,4-beta-Celobiosidase/química
Hypocrea/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Celulase/química
Celulose/química
Celulose 1,4-beta-Celobiosidase/genética
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9004-34-6 (Cellulose); EC 3.2.1.4 (Cellulase); EC 3.2.1.91 (Cellulose 1,4-beta-Cellobiosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE
[do] DOI:10.1093/protein/gzx036


  9 / 5606 MEDLINE  
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[PMID]:28869121
[Au] Autor:Yang M; Wang J; Hou X; Wu J; Fan X; Jiang F; Tao P; Wang F; Peng P; Yang F; Zhang J
[Ad] Endereço:College of Forestry, Northwest A&F University, 3 Taicheng Road, Yangling 712100, China.
[Ti] Título:Exploring surface characterization and electrostatic property of Hybrid Pennisetum during alkaline sulfite pretreatment for enhanced enzymatic hydrolysability.
[So] Source:Bioresour Technol;244(Pt 1):1166-1172, 2017 Nov.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The surface characterization and electrostatic property of Hybrid Pennisetum (HP) after alkaline sulfite pretreatment were explored for enhanced enzymatic hydrolysability. The O/C ratio in HP increased from 0.34 to 0.60, and C1 concentration decreased from 62.5% to 31.6%, indicating that alkaline sulfite pretreatment caused poorer lignin but richer carbohydrate on HP surface. Zeta potential and sulfur element analysis indicated that more enzymes would preferably adsorb on the carbohydrate surface of alkaline sulfite pretreated HP because the lignin was sulfonated, which facilitated the decrease of non-productive adsorption. Glucose yield of alkaline sulfite pretreated HP reached to 100% by synergistic action of cellulase and xylanase in the hydrolysis, which was significantly higher than that of NaOH pretreated, and the concentration of glucose released was 1.52times higher. The results suggested that alkaline sulfite pretreatment had potential for improving the HP hydrolysability, and the surface characterization and electrostatic property facilitated the enzymatic digestibility.
[Mh] Termos MeSH primário: Pennisetum
Sulfitos
[Mh] Termos MeSH secundário: Celulase
Hidrólise
Lignina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sulfites); 9005-53-2 (Lignin); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE


  10 / 5606 MEDLINE  
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[PMID]:28864903
[Au] Autor:Song EG; Ryu KH
[Ad] Endereço:Plant Virus GenBank, Department of Horticulture, Biotechnology and Landscape Architecture, Seoul Women's University, Seoul, Republic of Korea.
[Ti] Título:A pepper mottle virus-based vector enables systemic expression of endoglucanase D in non-transgenic plants.
[So] Source:Arch Virol;162(12):3717-3726, 2017 Dec.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Plant-virus-based expression vectors have been used as an alternative to the creation of transgenic plants. Using a virus-based vector, we investigated the feasibility of producing the endoglucanase D (EngD) from Clostridium cellulovorans in Nicotiana benthamiana. This protein has endoglucanase, xylanase, and exoglucanase activities and may be of value for cellulose digestion in the generation of biofuels from plant biomass. The EngD gene was cloned between the nuclear inclusion b (NIb)- and coat protein (CP)-encoding sequences of pSP6PepMoV-Vb1. In vitro transcripts derived from the clone (pSP6PepMoV-Vb1/EngD) were infectious in N. benthamiana but caused milder symptoms than wild-type PepMoV-Vb1. RT-PCR amplification of total RNA from non-inoculated upper leaves infected with PepMoV-Vb1/EngD produced the target band for the CP, partial NIb and EngD-CP regions of PepMoV-V1/EngD, in addition to nonspecific bands. Western blot analysis showed the CP target bands of PepMoV-Vb1/EngD as well as non-target bands. EngD enzymatic activity in infected plants was detected using a glucose assay. The plant leaves showed increased senescence compared with healthy and PepMoV-Vb1-infected plants. Our study suggests the feasibility of using a viral vector for systemic infection of plants for expression of heterologous engD for the purpose of digesting a cellulose substrate in plant cells for biomass production.
[Mh] Termos MeSH primário: Celulase/biossíntese
Clostridium cellulovorans/enzimologia
Expressão Gênica
Vetores Genéticos
Potyvirus/genética
Proteínas Recombinantes/biossíntese
Tabaco/enzimologia
[Mh] Termos MeSH secundário: Western Blotting
Celulase/genética
Clonagem Molecular
Clostridium cellulovorans/genética
Proteínas Recombinantes/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Tabaco/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3539-2



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