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[PMID]:29334221
[Au] Autor:Liu L; Gong W; Sun X; Chen G; Wang L
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University , 27 Shandanan Road, Jinan 250100, China.
[Ti] Título:Extracellular Enzyme Composition and Functional Characteristics of Aspergillus niger An-76 Induced by Food Processing Byproducts and Based on Integrated Functional Omics.
[So] Source:J Agric Food Chem;66(5):1285-1295, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Byproducts of food processing can be utilized for the production of high-value-added enzyme cocktails. In this study, we utilized integrated functional omics technology to analyze composition and functional characteristics of extracellular enzymes produced by Aspergillus niger grown on food processing byproducts. The results showed that oligosaccharides constituted by arabinose, xylose, and glucose in wheat bran were able to efficiently induce the production of extracellular enzymes of A. niger. Compared with other substrates, wheat bran was more effective at inducing the secretion of ß-glucosidases from GH1 and GH3 families, as well as >50% of proteases from A1-family aspartic proteases. Compared with proteins induced by single wheat bran or soybean dregs, the protein yield induced by their mixture was doubled, and the time required to reach peak enzyme activity was shortened by 25%. This study provided a technical platform for the complex formulation of various substrates and functional analysis of extracellular enzymes.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Aspergillus niger/crescimento & desenvolvimento
Indução Enzimática/efeitos dos fármacos
Manipulação de Alimentos
Oligossacarídeos/farmacologia
Resíduos
[Mh] Termos MeSH secundário: Arabinose/farmacologia
Ácido Aspártico Proteases/biossíntese
Celulases/biossíntese
Fibras na Dieta/análise
Grãos Comestíveis/química
Fermentação
Glucose/farmacologia
Glicosídeo Hidrolases/biossíntese
Peptídeo Hidrolases/biossíntese
Xilose/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dietary Fiber); 0 (Oligosaccharides); 0 (Waste Products); A1TA934AKO (Xylose); B40ROO395Z (Arabinose); EC 3.2.1.- (Cellulases); EC 3.2.1.- (Glycoside Hydrolases); EC 3.4.- (Aspartic Acid Proteases); EC 3.4.- (Peptide Hydrolases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180116
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05164


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[PMID]:29281693
[Au] Autor:Amaike Campen S; Lynn J; Sibert SJ; Srikrishnan S; Phatale P; Feldman T; Guenther JM; Hiras J; Tran YTA; Singer SW; Adams PD; Sale KL; Simmons BA; Baker SE; Magnuson JK; Gladden JM
[Ad] Endereço:Joint BioEnergy Institute (JBEI), Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, California, United States of America.
[Ti] Título:Expression of naturally ionic liquid-tolerant thermophilic cellulases in Aspergillus niger.
[So] Source:PLoS One;12(12):e0189604, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Efficient deconstruction of plant biomass is a major barrier to the development of viable lignocellulosic biofuels. Pretreatment with ionic liquids reduces lignocellulose recalcitrance to enzymatic hydrolysis, increasing yields of sugars for conversion into biofuels. However, commercial cellulases are not compatible with many ionic liquids, necessitating extensive water washing of pretreated biomass prior to hydrolysis. To circumvent this issue, previous research has demonstrated that several thermophilic bacterial cellulases can efficiently deconstruct lignocellulose in the presence of the ionic liquid, 1-ethyl-3-methylimadizolium acetate. As promising as these enzymes are, they would need to be produced at high titer in an industrial enzyme production host before they could be considered a viable alternative to current commercial cellulases. Aspergillus niger has been used to produce high titers of secreted enzymes in industry and therefore, we assessed the potential of this organism to be used as an expression host for these ionic liquid-tolerant cellulases. We demonstrated that 29 of these cellulases were expressed at detectable levels in a wild-type strain of A. niger, indicating a basic level of compatibility and potential to be produced at high levels in a host engineered to produce high titers of enzymes. We then profiled one of these enzymes in detail, the ß-glucosidase A5IL97, and compared versions expressed in both A. niger and Escherichia coli. This comparison revealed the enzymatic activity of A5IL97 purified from E. coli and A. niger is equivalent, suggesting that A. niger could be an excellent enzyme production host for enzymes originally characterized in E. coli, facilitating the transition from the laboratory to industry.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Celulases/metabolismo
Líquidos Iônicos/metabolismo
[Mh] Termos MeSH secundário: Biomassa
Celulases/genética
Escherichia coli/genética
Fermentação
Hidrólise
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Ionic Liquids); 0 (Recombinant Proteins); EC 3.2.1.- (Cellulases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189604


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[PMID]:29281673
[Au] Autor:Finlayson-Trick ECL; Getz LJ; Slaine PD; Thornbury M; Lamoureux E; Cook J; Langille MGI; Murray LE; McCormick C; Rohde JR; Cheng Z
[Ad] Endereço:Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada.
[Ti] Título:Taxonomic differences of gut microbiomes drive cellulolytic enzymatic potential within hind-gut fermenting mammals.
[So] Source:PLoS One;12(12):e0189404, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Host diet influences the diversity and metabolic activities of the gut microbiome. Previous studies have shown that the gut microbiome provides a wide array of enzymes that enable processing of diverse dietary components. Because the primary diet of the porcupine, Erethizon dorsatum, is lignified plant material, we reasoned that the porcupine microbiome would be replete with enzymes required to degrade lignocellulose. Here, we report on the bacterial composition in the porcupine microbiome using 16S rRNA sequencing and bioinformatics analysis. We extended this analysis to the microbiomes of 20 additional mammals located in Shubenacadie Wildlife Park (Nova Scotia, Canada), enabling the comparison of bacterial diversity amongst three mammalian taxonomic orders (Rodentia, Carnivora, and Artiodactyla). 16S rRNA sequencing was validated using metagenomic shotgun sequencing on selected herbivores (porcupine, beaver) and carnivores (coyote, Arctic wolf). In the microbiome, functionality is more conserved than bacterial composition, thus we mined microbiome data sets to identify conserved microbial functions across species in each order. We measured the relative gene abundances for cellobiose phosphorylase, endoglucanase, and beta-glucosidase to evaluate the cellulose-degrading potential of select mammals. The porcupine and beaver had higher proportions of genes encoding cellulose-degrading enzymes than the Artic wolf and coyote. These findings provide further evidence that gut microbiome diversity and metabolic capacity are influenced by host diet.
[Mh] Termos MeSH primário: Celulases/metabolismo
Fermentação
Intestinos/microbiologia
Mamíferos/metabolismo
Microbiota
[Mh] Termos MeSH secundário: Animais
Biodiversidade
Celulose/metabolismo
Intestinos/metabolismo
Mamíferos/classificação
RNA Ribossômico 16S/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Ribosomal, 16S); 9004-34-6 (Cellulose); EC 3.2.1.- (Cellulases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189404


  4 / 945 MEDLINE  
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[PMID]:28934551
[Au] Autor:Wright TA; Lucius Dougherty M; Schmitz B; Burridge KM; Makaroff K; Stewart JM; Fischesser HD; Shepherd JT; Berberich JA; Konkolewicz D; Page RC
[Ad] Endereço:Department of Chemistry and Biochemistry, 651 East High Street, Miami University , Oxford, Ohio 45056 United States.
[Ti] Título:Polymer Conjugation to Enhance Cellulase Activity and Preserve Thermal and Functional Stability.
[So] Source:Bioconjug Chem;28(10):2638-2645, 2017 Oct 18.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A thermophilic cellulase, FnCel5a, from Fervidobacterium nodosum was conjugated with various functional polymers including cationic, anionic, and strongly and weakly hydrogen bonding polymers. The activity of FnCel5a toward a high-molecular-weight carboxymethyl cellulose substrate was enhanced by polymer conjugation. Activity enhancements of 50% or greater observed for acrylamide and mixed N,N-dimethyl acrylamide-2-(N,N-dimethylamino)ethyl methacrylate polymers, suggesting that the greatest enhancements were caused by polymers capable of noncovalent interactions with the substrate. The conjugates were found to have nearly identical thermodynamic stability to the native enzyme, as assessed by free energy (ΔG), enthalpy (ΔH), and entropy (TΔS) parameters extracted from differential scanning fluorimetry. Polymers tended to confer comparable tolerance to high concentrations of dimethylformamide, with longer polymers typically enabling higher activity relative to shorter polymers. The new FnCel5a conjugates represent an advance in the production of cellulases that maintain activity at high temperatures or in the presence of denaturing organic solvents.
[Mh] Termos MeSH primário: Celulases/química
Celulases/metabolismo
Polímeros/química
Temperatura Ambiente
[Mh] Termos MeSH secundário: Entropia
Estabilidade Enzimática
Metacrilatos/química
Modelos Moleculares
Polimerização
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Methacrylates); 0 (Polymers); 1CS02G8656 (methacrylic acid); EC 3.2.1.- (Cellulases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00518


  5 / 945 MEDLINE  
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Rodriguez, Norberto Mario
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[PMID]:28850605
[Au] Autor:Abrão FO; Duarte ER; Pessoa MS; Santos VLD; Freitas Júnior LF; Barros KO; Hughes AFDS; Silva TD; Rodriguez NM
[Ad] Endereço:Instituto Federal Goiano, Ceres, Brasil.
[Ti] Título:Notable fibrolytic enzyme production by Aspergillus spp. isolates from the gastrointestinal tract of beef cattle fed in lignified pastures.
[So] Source:PLoS One;12(8):e0183628, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fungi have the ability to degrade vegetal cell wall carbohydrates, and their presence in the digestive tract of ruminants can minimize the effects of lignified forage on ruminal fermentation. Here, we evaluated enzyme production by Aspergillus spp. isolates from the digestive tracts of cattle grazed in tropical pastures during the dry season. Filamentous fungi were isolated from rumen and feces by culture in cellulose-based medium. Ninety fungal strains were isolated and identified by rDNA sequence analysis, microculture, or both. Aspergillus terreus was the most frequently isolated species, followed by Aspergillus fumigatus. The isolates were characterized with respect to their cellulolytic, xylanolytic, and lignolytic activity through qualitative evaluation in culture medium containing a specific corresponding carbon source. Carboxymethyl cellulase (CMCase) activity was quantified by the reducing sugar method. In the avicel and xilan degradation test, the enzyme activity (EA) at 48 h was significantly higher other periods (P < 0.05). Intra- and inter-specific differences in EA were verified, and high levels of phenoloxidases, which are crucial for lignin degradation, were observed in 28.9% of the isolates. Aspergillus terreus showed significantly higher EA for avicelase (3.96 ±1.77) and xylanase (3.13 ±.091) than the other Aspergillus species at 48 h of incubation. Isolates AT13 and AF69 showed the highest CMCase specific activity (54.84 and 33.03 U mg-1 protein, respectively). Selected Aspergillus spp. isolates produced remarkable levels of enzymes involved in vegetal cell wall degradation, suggesting their potential as antimicrobial additives or probiotics in ruminant diets.
[Mh] Termos MeSH primário: Aspergillus/enzimologia
Celulase/metabolismo
Celulases/metabolismo
Endo-1,4-beta-Xilanases/metabolismo
Trato Gastrointestinal/microbiologia
Lignina/metabolismo
[Mh] Termos MeSH secundário: Animais
Aspergillus/isolamento & purificação
Bovinos
Fezes/microbiologia
Rúmen/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9005-53-2 (Lignin); EC 3.2.1.- (Cellulases); EC 3.2.1.4 (Cellulase); EC 3.2.1.4 (carboxymethylcellulase); EC 3.2.1.8 (Endo-1,4-beta Xylanases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183628


  6 / 945 MEDLINE  
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[PMID]:28503798
[Au] Autor:Ben Hmad I; Gargouri A
[Ad] Endereço:Laboratory of Molecular Biology of Eukaryotes, Centre of Biotechnology of Sfax CBS/University of Sfax, Sfax, Tunisia.
[Ti] Título:Neutral and alkaline cellulases: Production, engineering, and applications.
[So] Source:J Basic Microbiol;57(8):653-658, 2017 Aug.
[Is] ISSN:1521-4028
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Neutral and alkaline cellulases from microorganisms constitute a major group of the industrial enzymes and find applications in various industries. Screening is the important ways to get novel cellulases. Most fungal cellulases have acidic pH optima, except some fungi like Humicola insolens species. However, new applications require the use of neutral and alkaline cellulases in food, brewery and wine, animal feed, textile and laundry, pulp and paper industries, agriculture as well in scientific research purposes. Indeed, the demand for these enzymes is growing more rapidly than ever before, and becomes the driving force for research on engineering the cellulolytic enzymes. Here, we present an overview of the biotechnological research for neutral and alkaline cellulases.
[Mh] Termos MeSH primário: Celulases/isolamento & purificação
Celulases/metabolismo
Microbiologia Industrial
[Mh] Termos MeSH secundário: Biotecnologia
Celulases/química
Fungos/enzimologia
Concentração de Íons de Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 3.2.1.- (Cellulases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170516
[St] Status:MEDLINE
[do] DOI:10.1002/jobm.201700111


  7 / 945 MEDLINE  
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[PMID]:28489493
[Au] Autor:Sornlake W; Rattanaphanjak P; Champreda V; Eurwilaichitr L; Kittisenachai S; Roytrakul S; Fujii T; Inoue H
[Ad] Endereço:a Bioresouces Technology Unit , National Center for Genetic Engineering and Biotechnology , Khlong Luang , Thailand.
[Ti] Título:Characterization of cellulolytic enzyme system of Schizophyllum commune mutant and evaluation of its efficiency on biomass hydrolysis.
[So] Source:Biosci Biotechnol Biochem;81(7):1289-1299, 2017 Jul.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Schizophyllum commune is a basidiomycete equipped with an efficient cellulolytic enzyme system capable of growth on decaying woods. In this study, production of lignocellulose-degrading enzymes from S. commune mutant G-135 (SC-Cel) on various cellulosic substrates was examined. The highest cellulase activities including CMCase, FPase, and ß-glucosidase were obtained on Avicel-PH101 while a wider range of enzymes attacking non-cellulosic polysaccharides and lignin were found when grown on alkaline-pretreated biomass. Proteomic analysis of SC-Cel also revealed a complex enzyme system comprising seven glycosyl hydrolase families with an accessory carbohydrate esterase, polysaccharide lyase, and auxiliary redox enzymes. SC-Cel obtained on Avicel-PH101 effectively hydrolyzed all agricultural residues with the maximum glucan conversion of 98.0% using corn cobs with an enzyme dosage of 5 FPU/g-biomass. The work showed potential of SC-Cel on hydrolysis of various herbaceous biomass with enhanced efficiency by addition external ß-xylosidase.
[Mh] Termos MeSH primário: Celulases/química
Celulose/química
Proteínas Fúngicas/química
Lignina/química
Proteoma/secreção
Schizophyllum/química
[Mh] Termos MeSH secundário: Biomassa
Celulases/isolamento & purificação
Celulose/metabolismo
Fermentação
Proteínas Fúngicas/isolamento & purificação
Expressão Gênica
Hidrólise
Isoenzimas/química
Isoenzimas/isolamento & purificação
Lignina/metabolismo
Mutação
Oryza/química
Proteoma/genética
Saccharum/química
Schizophyllum/enzimologia
Schizophyllum/genética
Resíduos
Madeira/química
Xilosidases/química
Zea mays/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Isoenzymes); 0 (Proteome); 0 (Waste Products); 11132-73-3 (lignocellulose); 9004-34-6 (Cellulose); 9005-53-2 (Lignin); EC 3.2.1.- (Cellulases); EC 3.2.1.- (Xylosidases); EC 3.2.1.37 (exo-1,4-beta-D-xylosidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170707
[Lr] Data última revisão:
170707
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170511
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1320937


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[PMID]:28319769
[Au] Autor:Xue Y; Wang X; Chen X; Hu J; Gao MT; Li J
[Ad] Endereço:Shanghai Key Laboratory of Bio-energy Crops, School of Life Sciences, Shanghai University, 99 Shangda Road, Shanghai 200444, China.
[Ti] Título:Effects of different cellulases on the release of phenolic acids from rice straw during saccharification.
[So] Source:Bioresour Technol;234:208-216, 2017 Jun.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Effects of different cellulases on the release of phenolic acids from rice straw during saccharification were investigated in this study. All cellulases tested increased the contents of phenolic acids during saccharification. However, few free phenolic acids were detected, as they were present in conjugated form after saccharification when the cellulases from Trichoderma reesei, Trichoderma viride and Aspergillus niger were used. On the other hand, phenolic acids were present in free form when the Acremonium cellulolyticus cellulase was used. Assays of enzyme activity showed that, besides high cellulase activity, the A. cellulolyticus cellulase exhibited high feruloyl esterase (FAE) activity. A synergistic interaction between FAE and cellulase led to the increase in free phenolic acids, and thus an increase in antioxidative and antiradical activities of the phenolic acids. Moreover, a cost estimation demonstrated the feasibility of phenolic acids as value-added products to reduce the total production cost of ethanol.
[Mh] Termos MeSH primário: Oryza
[Mh] Termos MeSH secundário: Aspergillus niger
Celulase
Celulases
Trichoderma/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.- (Cellulases); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170321
[St] Status:MEDLINE


  9 / 945 MEDLINE  
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[PMID]:28290772
[Au] Autor:Tani S; Yuki S; Kunitake E; Sumitani JI; Kawaguchi T
[Ad] Endereço:a Graduate School of Life and Environmental Sciences , Osaka Prefecture University , Sakai , Japan.
[Ti] Título:Dipeptidyl peptidase IV is involved in the cellulose-responsive induction of cellulose biomass-degrading enzyme genes in Aspergillus aculeatus.
[So] Source:Biosci Biotechnol Biochem;81(6):1227-1234, 2017 Jun.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We screened for factors involved in the cellulose-responsive induction of cellulose biomass-degrading enzyme genes from approximately 12,000 Aspergillus aculeatus T-DNA insertion mutants harboring a transcriptional fusion between the FIII-avicelase gene (cbhI) promoter and the orotidine 5'-monophosphate decarboxylase gene. Analysis of 5-fluoroorodic acid (5-FOA) sensitivity, cellulose utilization, and cbhI expression of the mutants revealed that a mutant harboring T-DNA at the dipeptidyl peptidase IV (dppIV) locus had acquired 5-FOA resistance and was deficient in cellulose utilization and cbhI expression. The deletion of dppIV resulted in a significant reduction in the cellulose-responsive expression of both cbhI as well as genes controlled by XlnR-independent and XlnR-dependent signaling pathways at an early phase in A. aculeatus. In contrast, the dppIV deletion did not affect the xylose-responsive expression of genes under the control of XlnR. These results demonstrate that DppIV participates in cellulose-responsive induction in A. aculeatus.
[Mh] Termos MeSH primário: Aspergillus/genética
Celulases/genética
Celulose/metabolismo
Dipeptidil Peptidase 4/genética
Proteínas Fúngicas/genética
Regulação Fúngica da Expressão Gênica
Orotidina-5´-Fosfato Descarboxilase/genética
[Mh] Termos MeSH secundário: Aspergillus/efeitos dos fármacos
Aspergillus/enzimologia
Celulases/metabolismo
Celulose/farmacologia
DNA Bacteriano/genética
DNA Bacteriano/metabolismo
Dipeptidil Peptidase 4/agonistas
Dipeptidil Peptidase 4/metabolismo
Proteínas Fúngicas/metabolismo
Deleção de Genes
Mutagênese Insercional
Ácido Orótico/análogos & derivados
Ácido Orótico/metabolismo
Ácido Orótico/farmacologia
Orotidina-5'-Fosfato Descarboxilase/metabolismo
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Transdução de Sinais
Xilose/metabolismo
Xilose/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Fungal Proteins); 0 (Recombinant Fusion Proteins); 0 (T-DNA); 61H4T033E5 (Orotic Acid); 7IA9OUC93E (5-fluoroorotic acid); 9004-34-6 (Cellulose); A1TA934AKO (Xylose); EC 3.2.1.- (Cellulases); EC 3.4.14.5 (Dipeptidyl Peptidase 4); EC 4.1.1.23 (Orotidine-5'-Phosphate Decarboxylase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170703
[Lr] Data última revisão:
170703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170315
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1295800


  10 / 945 MEDLINE  
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[PMID]:28282268
[Au] Autor:Song HT; Yang YM; Liu DK; Xu XQ; Xiao WJ; Liu ZL; Xia WC; Wang CY; Yu X; Jiang ZB
[Ad] Endereço:a Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, Hubei University , Wuhan , China.
[Ti] Título:Construction of recombinant Yarrowia lipolytica and its application in bio-transformation of lignocellulose.
[So] Source:Bioengineered;8(5):624-629, 2017 Sep 03.
[Is] ISSN:2165-5987
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lignocellulose is a polysaccharide and an abundant biomass resource that widely exists in grains, beans, rice, and their by-products. Over 10 million tons of lignocellulose resources and processing products are produced every year in China. Three recombinant Y. lipolytica strains with cellulase (ß-glucosidase, endoglucanase and cellobiohydrolase) were constructed. The enzymatic activities of these enzymes were 14.181 U/mL, 16.307 U/mL, and 17.391 U/mL, respectively. The whole cell cellulases were used for a stover bio-transformation. The celluloses in the stover were partly degraded by the cellulases, and the degradation products were transformed into single cell protein (SCP) by the Y. lipolytica cells. After 15 d of fermentation with the whole cell cellulases, the protein content of the maize stover and the rice straw reached 16.23% and 14.75%, which increased by 168.26% and 161.52% compared with the control, respectively. This study provides a new stage for the efficient utilization of stover in the feed industry.
[Mh] Termos MeSH primário: Celulases/genética
Lignina/metabolismo
Engenharia Metabólica/métodos
Oryza/microbiologia
Recombinação Genética/genética
Yarrowia/fisiologia
[Mh] Termos MeSH secundário: Biotransformação/genética
Melhoramento Genético/métodos
Componentes Aéreos da Planta/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
11132-73-3 (lignocellulose); 9005-53-2 (Lignin); EC 3.2.1.- (Cellulases)
[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:170311
[St] Status:MEDLINE
[do] DOI:10.1080/21655979.2017.1293219



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