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Pesquisa : D09.947.875.627 [Categoria DeCS]
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[PMID]:28780268
[Au] Autor:Freitas BCB; Morais MG; Costa JAV
[Ad] Endereço:College of Chemistry and Food Engineering, Federal University of Rio Grande, Laboratory of Biochemical Engineering, Rio Grande, RS, Brazil.
[Ti] Título:Chlorella minutissima cultivation with CO and pentoses: Effects on kinetic and nutritional parameters.
[So] Source:Bioresour Technol;244(Pt 1):338-344, 2017 Nov.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CO emissions and the large quantity of lignocellulosic waste generated by industrialized nations constitute problems that may affect human health as well as the global economy. The objective of this work was to evaluate the effects of using CO and pentoses on the growth, protein profile, carbohydrate content and potential ethanol production by fermentation of Chlorella minutissima biomass. CO and pentose supplementation can induce changes in the microalgal protein profile. A biomass production of 1.84g.L and a CO biofixation rate of 274.63mg.L .d were obtained with the use of 20% (v.v ) CO . For cultures with 20% (v.v ) CO and reduced nitrogen, the carbohydrate content was 52.3% (w.w ), and theoretically, 33.9mL.100g of ethanol can be produced. These results demonstrate that C. minutissima cultured with the combined use of CO and pentoses generates a biomass with high bioenergetic potential.
[Mh] Termos MeSH primário: Dióxido de Carbono
Chlorella
Pentoses
[Mh] Termos MeSH secundário: Biomassa
Seres Humanos
Microalgas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pentoses); 142M471B3J (Carbon Dioxide)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170807
[St] Status:MEDLINE


  2 / 1314 MEDLINE  
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[PMID]:28249101
[Au] Autor:Kolbe K; Möckl L; Sohst V; Brandenburg J; Engel R; Malm S; Bräuchle C; Holst O; Lindhorst TK; Reiling N
[Ad] Endereço:Otto Diels Institute of Organic Chemistry, Christiana Albertina University of Kiel, Otto-Hahn-Platz 3-4, 24118, Kiel, Germany.
[Ti] Título:Azido Pentoses: A New Tool To Efficiently Label Mycobacterium tuberculosis Clinical Isolates.
[So] Source:Chembiochem;18(13):1172-1176, 2017 Jul 04.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Mycobacterium tuberculosis (Mtb), the main causative agent of tuberculosis (Tb), has a complex cell envelope which forms an efficient barrier to antibiotics, thus contributing to the challenges of anti-tuberculosis therapy. However, the unique Mtb cell wall can be considered an advantage and be utilized to selectively label Mtb bacteria. Here we introduce three azido pentoses as new compounds for metabolic labeling of Mtb: 3-azido arabinose (3AraAz), 3-azido ribose (3RiboAz), and 5-azido arabinofuranose (5AraAz). 5AraAz demonstrated the highest level of Mtb labeling and was efficiently incorporated into the Mtb cell wall. All three azido pentoses can be easily used to label a variety of Mtb clinical isolates without influencing Mtb-dependent phagosomal maturation arrest in infection studies with human macrophages. Thus, this metabolic labeling method offers the opportunity to attach desired molecules to the surface of Mtb bacteria in order to facilitate investigation of the varying virulence characteristics of different Mtb clinical isolates, which influence the outcome of a Tb infection.
[Mh] Termos MeSH primário: Azidas/química
Parede Celular/química
Mycobacterium tuberculosis/química
Pentoses/química
Coloração e Rotulagem/métodos
[Mh] Termos MeSH secundário: Biomarcadores/metabolismo
Parede Celular/metabolismo
Citometria de Fluxo
Expressão Gênica
Seres Humanos
Glicoproteínas de Membrana Associadas ao Lisossomo/genética
Glicoproteínas de Membrana Associadas ao Lisossomo/imunologia
Macrófagos/citologia
Macrófagos/imunologia
Mycobacterium tuberculosis/metabolismo
Fagocitose
Proteínas rab5 de Ligação ao GTP/genética
Proteínas rab5 de Ligação ao GTP/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azides); 0 (Biomarkers); 0 (LAMP1 protein, human); 0 (Lysosome-Associated Membrane Glycoproteins); 0 (Pentoses); EC 3.6.1.- (RAB5C protein, human); EC 3.6.5.2 (rab5 GTP-Binding Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201600706


  3 / 1314 MEDLINE  
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[PMID]:28154188
[Au] Autor:Gunn LH; Valegård K; Andersson I
[Ad] Endereço:From the Department of Cell and Molecular Biology, Uppsala University, S-751 24 Uppsala, Sweden laura.gunn@icm.uu.se.
[Ti] Título:A unique structural domain in ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic.
[So] Source:J Biol Chem;292(16):6838-6850, 2017 Apr 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The catalytic inefficiencies of the CO -fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) often limit plant productivity. Strategies to engineer more efficient plant Rubiscos have been hampered by evolutionary constraints, prompting interest in Rubisco isoforms from non-photosynthetic organisms. The methanogenic archaeon contains a Rubisco isoform that functions to scavenge the ribulose-1,5-bisphosphate (RuBP) by-product of purine/pyrimidine metabolism. The crystal structure of Rubisco (MbR) presented here at 2.6 Å resolution is composed of catalytic large subunits (LSu) assembled into pentamers of dimers, (L ) , and differs from Rubiscos from higher plants where LSus are glued together by small subunits (SSu) into hexadecameric L S enzymes. MbR contains a unique 29-amino acid insertion near the C terminus, which folds as a separate domain in the structure. This domain, which is visualized for the first time in this study, is located in a similar position to SSus in L S enzymes between LSus of adjacent L dimers, where negatively charged residues coordinate around a Mg ion in a fashion that suggests this domain may be important for the assembly process. The Rubisco assembly domain is thus an inbuilt SSu mimic that concentrates L dimers. MbR assembly is ligand-stimulated, and we show that only 6-carbon molecules with a particular stereochemistry at the C carbon can induce oligomerization. Based on MbR structure, subunit arrangement, sequence, phylogenetic distribution, and function, MbR and a subset of Rubiscos from the Methanosarcinales order are proposed to belong to a new Rubisco subgroup, named form IIIB.
[Mh] Termos MeSH primário: Methanosarcinaceae/enzimologia
Ribulose-Bifosfato Carboxilase/química
Ribulosefosfatos/química
[Mh] Termos MeSH secundário: Carbono/química
Domínio Catalítico
Clonagem Molecular
Cristalografia por Raios X
Escherichia coli/metabolismo
Ligantes
Mutagênese Sítio-Dirigida
Pentoses/química
Filogenia
Domínios Proteicos
Dobramento de Proteína
Multimerização Proteica
Ribulose-Bifosfato Carboxilase/metabolismo
Spinacia oleracea/enzimologia
Eletricidade Estática
Estereoisomerismo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ligands); 0 (Pentoses); 0 (Ribulosephosphates); 2002-28-0 (ribulose-1,5 diphosphate); 5556-48-9 (ribulose); 7440-44-0 (Carbon); EC 4.1.1.39 (Ribulose-Bisphosphate Carboxylase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.767145


  4 / 1314 MEDLINE  
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[PMID]:28139224
[Au] Autor:Myrgorodska I; Javelle T; Meinert C; Meierhenrich UJ
[Ad] Endereço:Université Côte d'Azur, CNRS, Institut de Chimie de Nice UMR 7272, Nice, France; Synchrotron SOLEIL, France.
[Ti] Título:Enantioresolution and quantification of monosaccharides by comprehensive two-dimensional gas chromatography.
[So] Source:J Chromatogr A;1487:248-253, 2017 Mar 03.
[Is] ISSN:1873-3778
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This work presents the development of a simple and efficient analytical protocol for the direct enantioselective resolution of sugars. A racemic mixture of the C3 sugar d,l-glyceraldehyde and the C5 monosaccharides d,l-arabinose, d,l-ribose, d,l-xylose, and d,l-lyxose was subjected to derivatization with trifluoroacetic anhydride, and corresponding derivatives were separated on a ß-cyclodextrin column with excellent resolution factors. Even though each aldopentose shows beside the linear form four predominant cyclic hemiacetals being the α- and ß-furanose along with the α- and ß-pyranose, we show that the overall enantiomeric excess of each compound can be precisely determined. Moreover, the measured detection limit for derivatized aldopentoses ranges from 0.015 to 0.019pmol on the column, while the quantification limit varies from 0.5 to 0.64pmol on the column.
[Mh] Termos MeSH primário: Cromatografia Gasosa/métodos
Monossacarídeos/análise
[Mh] Termos MeSH secundário: Arabinose/análise
Arabinose/isolamento & purificação
Monossacarídeos/química
Monossacarídeos/isolamento & purificação
Pentoses/análise
Pentoses/isolamento & purificação
Ribose/análise
Ribose/isolamento & purificação
Estereoisomerismo
Xilose/análise
Xilose/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Monosaccharides); 0 (Pentoses); 65-42-9 (lyxose); 681HV46001 (Ribose); A1TA934AKO (Xylose); B40ROO395Z (Arabinose)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170314
[Lr] Data última revisão:
170314
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


  5 / 1314 MEDLINE  
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[PMID]:27909055
[Au] Autor:Singh C; Glaab E; Linster CL
[Ad] Endereço:From the Luxembourg Centre for Systems Biomedicine, University of Luxembourg, L-4362 Esch-sur-Alzette, Luxembourg.
[Ti] Título:Molecular Identification of d-Ribulokinase in Budding Yeast and Mammals.
[So] Source:J Biol Chem;292(3):1005-1028, 2017 Jan 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteomes of even well characterized organisms still contain a high percentage of proteins with unknown or uncertain molecular and/or biological function. A significant fraction of those proteins is predicted to have catalytic properties. Here we aimed at identifying the function of the Saccharomyces cerevisiae Ydr109c protein and its human homolog FGGY, both of which belong to the broadly conserved FGGY family of carbohydrate kinases. Functionally identified members of this family phosphorylate 3- to 7-carbon sugars or sugar derivatives, but the endogenous substrate of S. cerevisiae Ydr109c and human FGGY has remained unknown. Untargeted metabolomics analysis of an S. cerevisiae deletion mutant of YDR109C revealed ribulose as one of the metabolites with the most significantly changed intracellular concentration as compared with a wild-type strain. In human HEK293 cells, ribulose could only be detected when ribitol was added to the cultivation medium, and under this condition, FGGY silencing led to ribulose accumulation. Biochemical characterization of the recombinant purified Ydr109c and FGGY proteins showed a clear substrate preference of both kinases for d-ribulose over a range of other sugars and sugar derivatives tested, including l-ribulose. Detailed sequence and structural analyses of Ydr109c and FGGY as well as homologs thereof furthermore allowed the definition of a 5-residue d-ribulokinase signature motif (TCSLV). The physiological role of the herein identified eukaryotic d-ribulokinase remains unclear, but we speculate that S. cerevisiae Ydr109c and human FGGY could act as metabolite repair enzymes, serving to re-phosphorylate free d-ribulose generated by promiscuous phosphatases from d-ribulose 5-phosphate. In human cells, FGGY can additionally participate in ribitol metabolism.
[Mh] Termos MeSH primário: Pentoses/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Proteínas/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Inativação Gênica
Células HEK293
Seres Humanos
Pentoses/genética
Fosforilação
Fosfotransferases (Aceptor do Grupo Álcool)/química
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Proteínas/química
Proteínas/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (FLJ10986 protein, human); 0 (Pentoses); 0 (Proteins); 0 (Saccharomyces cerevisiae Proteins); 5556-48-9 (ribulose); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.47 (D-ribulokinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161203
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.760744


  6 / 1314 MEDLINE  
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[PMID]:27878973
[Au] Autor:Aristilde L
[Ad] Endereço:Department of Biological and Environmental Engineering, College of Agriculture and Life Sciences, Cornell University, Ithaca, NY, 14853, USA.
[Ti] Título:Metabolite labelling reveals hierarchies in Clostridium acetobutylicum that selectively channel carbons from sugar mixtures towards biofuel precursors.
[So] Source:Microb Biotechnol;10(1):162-174, 2017 Jan.
[Is] ISSN:1751-7915
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Clostridial fermentation of cellulose and hemicellulose relies on the cellular physiology controlling the metabolism of the cellulosic hexose sugar (glucose) with respect to the hemicellulosic pentose sugars (xylose and arabinose) and the hemicellulosic hexose sugars (galactose and mannose). Here, liquid chromatography-mass spectrometry and stable isotope tracers in Clostridium acetobutylicum were applied to investigate the metabolic hierarchy of glucose relative to the different hemicellulosic sugars towards two important biofuel precursors, acetyl-coenzyme A and butyryl-coenzyme A. The findings revealed constitutive metabolic hierarchies in C. acetobutylicum that facilitate (i) selective investment of hemicellulosic pentoses towards ribonucleotide biosynthesis without substantial investment into biofuel production and (ii) selective contribution of hemicellulosic hexoses through the glycolytic pathway towards biofuel precursors. Long-term isotopic enrichment demonstrated incorporation of both pentose sugars into pentose-phosphates and ribonucleotides in the presence of glucose. Kinetic labelling data, however, showed that xylose was not routed towards the biofuel precursors but there was minor contribution from arabinose. Glucose hierarchy over the hemicellulosic hexoses was substrate-dependent. Kinetic labelling of hexose-phosphates and triose-phosphates indicated that mannose was assimilated but not galactose. Labelling of both biofuel precursors confirmed this metabolic preference. These results highlight important metabolic considerations in the accounting of clostridial mixed-sugar utilization.
[Mh] Termos MeSH primário: Biocombustíveis
Carbono/metabolismo
Clostridium acetobutylicum/metabolismo
Hexoses/metabolismo
Análise do Fluxo Metabólico
Pentoses/metabolismo
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Acil Coenzima A/metabolismo
Biotransformação
Celulose/metabolismo
Cromatografia Líquida
Marcação por Isótopo
Espectrometria de Massas
Ribonucleotídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Biofuels); 0 (Hexoses); 0 (Pentoses); 0 (Ribonucleotides); 2140-48-9 (butyryl-coenzyme A); 72-89-9 (Acetyl Coenzyme A); 7440-44-0 (Carbon); 9004-34-6 (Cellulose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161124
[St] Status:MEDLINE
[do] DOI:10.1111/1751-7915.12459


  7 / 1314 MEDLINE  
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[PMID]:27816753
[Au] Autor:Rasineni GK; Loh PC; Lim BH
[Ad] Endereço:Department of Biochemistry, University of Nebraska Lincoln, NE 68588, USA; Department of Plant Sciences, University of Hyderabad, Telangana 500 046, India.
[Ti] Título:Characterization of Chlamydomonas Ribulose-1,5-bisphosphate carboxylase/oxygenase variants mutated at residues that are post-translationally modified.
[So] Source:Biochim Biophys Acta;1861(2):79-85, 2017 02.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the chloroplast enzyme that fixes CO in photosynthesis, but the enzyme also fixes O , which leads to the wasteful photorespiratory pathway. If we better understand the structure-function relationship of the enzyme, we might be able to engineer improvements. When the crystal structure of Chlamydomonas Rubisco was solved, four new posttranslational modifications were observed which are not present in other species. The modifications were 4-hydroxylation of the conserved Pro-104 and 151 residues, and S-methylation of the variable Cys-256 and 369 residues, which are Phe-256 and Val-369 in land plants. Because the modifications were only observed in Chlamydomonas Rubisco, they might account for the differences in kinetic properties between the algal and plant enzymes. METHODS: Site-directed mutagenesis and chloroplast transformation have been used to test the essentiality of these modifications by replacing each of the residues with alanine (Ala). Biochemical analyses were done to determine the specificity factors and kinetic constants. RESULTS: Replacing the modified-residues in Chlamydomonas Rubisco affected the enzyme's catalytic activity. Substituting hydroxy-Pro-104 and methyl-Cys-256 with alanine influenced Rubisco catalysis. CONCLUSION: This is the first study on these posttranslationally-modified residues in Rubisco by genetic engineering. As these forms of modifications/regulation are not available in plants, the modified residues could be a means to modulate Rubisco activity. GENERAL SIGNIFICANCE: With a better understanding of Rubisco structure-function, we can define targets for improving the enzyme.
[Mh] Termos MeSH primário: Chlamydomonas reinhardtii/genética
Mutação/genética
Oxigenases/genética
Processamento de Proteína Pós-Traducional/genética
Ribulosefosfatos/genética
[Mh] Termos MeSH secundário: Alanina/genética
Catálise
Cloroplastos/genética
Engenharia Genética/métodos
Cinética
Mutagênese Sítio-Dirigida/métodos
Pentoses/genética
Fotossíntese/genética
Ribulose-Bifosfato Carboxilase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pentoses); 0 (Ribulosephosphates); 2002-28-0 (ribulose-1,5 diphosphate); 5556-48-9 (ribulose); EC 1.13.- (Oxygenases); EC 4.1.1.39 (Ribulose-Bisphosphate Carboxylase); OF5P57N2ZX (Alanine)
[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:161107
[St] Status:MEDLINE


  8 / 1314 MEDLINE  
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[PMID]:27506274
[Au] Autor:Sukpipat W; Komeda H; Prasertsan P; Asano Y
[Ad] Endereço:Department of Industrial Biotechnology, Faculty of Agro-Industry, Prince of Songkla University, Songkhla 90112, Thailand; Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan.
[Ti] Título:Purification and characterization of xylitol dehydrogenase with l-arabitol dehydrogenase activity from the newly isolated pentose-fermenting yeast Meyerozyma caribbica 5XY2.
[So] Source:J Biosci Bioeng;123(1):20-27, 2017 Jan.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Meyerozyma caribbica strain 5XY2, which was isolated from an alcohol fermentation starter in Thailand, was found to catabolize l-arabinose as well as d-glucose and d-xylose. The highest production amounts of ethanol from d-glucose, xylitol from d-xylose, and l-arabitol from l-arabinose were 0.45 g/g d-glucose, 0.60 g/g d-xylose, and 0.61 g/g l-arabinose with 21.7 g/L ethanol, 20.2 g/L xylitol, and 30.3 g/l l-arabitol, respectively. The enzyme with l-arabitol dehydrogenase (LAD) activity was purified from the strain and found to exhibit broad specificity to polyols, such as xylitol, d-sorbitol, ribitol, and l-arabitol. Xylitol was the preferred substrate with K =16.1 mM and k /K =67.0 min mM , while l-arabitol was also a substrate for the enzyme with K =31.1 mM and k /K =6.5 min mM . Therefore, this enzyme from M. caribbica was named xylitol dehydrogenase (McXDH). McXDH had an optimum temperature and pH at 40°C and 9.5, respectively. The McXDH gene included a coding sequence of 1086 bp encoding a putative 362 amino acid protein of 39 kDa with an apparent homopentamer structure. Native McXDH and recombinant McXDH exhibited relative activities toward l-arabitol of approximately 20% that toward xylitol, suggesting the applicability of this enzyme with the functions of XDH and LAD to the development of pentose-fermenting Saccharomyces cerevisiae.
[Mh] Termos MeSH primário: D-Xilulose Redutase/isolamento & purificação
D-Xilulose Redutase/metabolismo
Fermentação
Pentoses/metabolismo
Saccharomycetales/metabolismo
Desidrogenase do Álcool de Açúcar/metabolismo
[Mh] Termos MeSH secundário: Etanol/metabolismo
Glucose/metabolismo
Oxirredução
Saccharomycetales/enzimologia
Álcoois Açúcares/metabolismo
Xilitol/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pentoses); 0 (Sugar Alcohols); 3K9958V90M (Ethanol); EC 1.1.- (Sugar Alcohol Dehydrogenases); EC 1.1.1.11 (D-arabinitol dehydrogenase); EC 1.1.1.9 (D-Xylulose Reductase); IY9XDZ35W2 (Glucose); VCQ006KQ1E (Xylitol)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160811
[St] Status:MEDLINE


  9 / 1314 MEDLINE  
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[PMID]:27271725
[Au] Autor:Yang W; Jiang Z; Liu L; Lin Y; Wang L; Zhou S
[Ad] Endereço:School of Food Science and Technology in Jiangnan University, Wuxi, Jiangsu, 214122, China.
[Ti] Título:The effect of pentosanase on the solubilisation and degradation of arabinoxylan extracted from whole and refined wheat flour.
[So] Source:J Sci Food Agric;97(3):1034-1041, 2017 Feb.
[Is] ISSN:1097-0010
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The quality improvement capability of pentosanase (Pn) for whole-wheat Chinese steamed bread (CSB) is not as efficient as that for refined CSB. However, the underlying mechanism remains to be elucidated. In this work, water-extractable arabinoxylan (WEAX) and water-unextractable solids (WUS) were extracted from whole and refined wheat flour, and then treated with Pn under the conditions similar to CSB-making. Solubilisation and degradation of arabinoxylan (AX) caused by Pn treatment were determined. RESULTS: WEAX from whole flour exhibited higher molecular weight than that from refined flour before and after the treatment with equivalent Pn. Compared with WUS from refined flour, WUS from whole flour had a much lower dissolution degree but the degradation of AX released from the WUS was more efficiently. Moreover, AX released from WUS for refined flour showed a higher Ara/Xyl ratio and the percentage of residual ferulic acid in WUS decreased more significantly. CONCLUSION: The difference in quality improvement degree for Pn in whole-wheat and refined CSB might be mainly explained by its effect on WUS. That is, Pn contributed much more to the solubilisation of WUS from refined flour but provoked degradation predominantly on AX solubilised from WUS isolated from whole flour. © 2016 Society of Chemical Industry.
[Mh] Termos MeSH primário: Pão/análise
Farinha/análise
Qualidade dos Alimentos
Triticum/química
Grãos Integrais/química
Xilanos/metabolismo
Xilosidases/metabolismo
[Mh] Termos MeSH secundário: Fenômenos Químicos
China
Culinária
Ácidos Cumáricos/análise
Eurotiales/enzimologia
Manipulação de Alimentos
Proteínas Fúngicas/metabolismo
Hidrólise
Fenômenos Mecânicos
Peso Molecular
Pentoses/metabolismo
Solubilidade
Vapor
Especificidade por Substrato
Viscosidade
Xilanos/química
Xilanos/isolamento & purificação
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coumaric Acids); 0 (Fungal Proteins); 0 (Pentoses); 0 (Steam); 0 (Xylans); 9040-27-1 (arabinoxylan); AVM951ZWST (ferulic acid); EC 3.2.1.- (Xylosidases); EC 3.2.1.- (arabinoxylanase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE
[do] DOI:10.1002/jsfa.7833


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[PMID]:27805580
[Au] Autor:Slininger PJ; Shea-Andersh MA; Thompson SR; Dien BS; Kurtzman CP; Sousa LD; Balan V
[Ad] Endereço:Bioenergy Research Unit, National Center for Agricultural Utilization Research; Pat.Slininger@ars.usda.gov.
[Ti] Título:Techniques for the Evolution of Robust Pentose-fermenting Yeast for Bioconversion of Lignocellulose to Ethanol.
[So] Source:J Vis Exp;(116), 2016 Oct 24.
[Is] ISSN:1940-087X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lignocellulosic biomass is an abundant, renewable feedstock useful for production of fuel-grade ethanol and other bio-products. Pretreatment and enzyme saccharification processes release sugars that can be fermented by yeast. Traditional industrial yeasts do not ferment xylose (comprising up to 40% of plant sugars) and are not able to function in concentrated hydrolyzates. Concentrated hydrolyzates are needed to support economical ethanol recovery, but they are laden with toxic byproducts generated during pretreatment. While detoxification methods can render hydrolyzates fermentable, they are costly and generate waste disposal liabilities. Here, adaptive evolution and isolation techniques are described and demonstrated to yield derivatives of the native Scheffersomyces stipitis strain NRRL Y-7124 that are able to efficiently convert hydrolyzates to economically recoverable ethanol despite adverse culture conditions. Improved individuals are enriched in an evolving population using multiple selection pressures reliant on natural genetic diversity of the S. stipitis population and mutations induced by exposures to two diverse hydrolyzates, ethanol or UV radiation. Final evolution cultures are dilution plated to harvest predominant isolates, while intermediate populations, frozen in glycerol at various stages of evolution, are enriched on selective media using appropriate stress gradients to recover most promising isolates through dilution plating. Isolates are screened on various hydrolyzate types and ranked using a novel procedure involving dimensionless relative performance index (RPI) transformations of the xylose uptake rate and ethanol yield data. Using the RPI statistical parameter, an overall relative performance average is calculated to rank isolates based on multiple factors, including culture conditions (varying in nutrients and inhibitors) and kinetic characteristics. Through application of these techniques, derivatives of the parent strain had the following improved features in enzyme saccharified hydrolyzates at pH 5-6: reduced initial lag phase preceding growth, reduced diauxic lag during glucose-xylose transition, significantly enhanced fermentation rates, improved ethanol tolerance and accumulation to 40 g/L.
[Mh] Termos MeSH primário: Pentoses
Saccharomyces cerevisiae
[Mh] Termos MeSH secundário: Etanol
Fermentação
Xilose
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Pentoses); 3K9958V90M (Ethanol); A1TA934AKO (Xylose)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE
[do] DOI:10.3791/54227



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