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  1 / 3877 MEDLINE  
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[PMID]:29324789
[Au] Autor:Choi JH; Shin KC; Oh DK
[Ad] Endereço:Department of Bioscience and Biotechnology, Konkuk University, Seoul, Republic of Korea.
[Ti] Título:An L213A variant of ß-glycosidase from Sulfolobus solfataricus with increased α-L-arabinofuranosidase activity converts ginsenoside Rc to compound K.
[So] Source:PLoS One;13(1):e0191018, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Compound K (C-K) is a crucial pharmaceutical and cosmetic component because of disease prevention and skin anti-aging effects. For industrial application of this active compound, the protopanaxadiol (PPD)-type ginsenosides should be transformed to C-K. ß-Glycosidase from Sulfolobus solfataricus has been reported as an efficient C-K-producing enzyme, using glycosylated PPD-type ginsenosides as substrates. ß-Glycosidase from S. solfataricus can hydrolyze ß-d-glucopyranoside in ginsenosides Rc, C-Mc1, and C-Mc, but not α-l-arabinofuranoside in these ginsenosides. To determine candidate residues involved in α-l-arabinofuranosidase activity, compound Mc (C-Mc) was docking to ß-glycosidase from S. solfataricus in homology model and sequence was aligned with ß-glycosidase from Pyrococcus furiosus that has α-l-arabinofuranosidase activity. A L213A variant ß-glycosidase with increased α-l-arabinofuranosidase activity was selected by substitution of other amino acids for candidate residues. The increased α-l-arabinofuranosidase activity of the L213A variant was confirmed through the determination of substrate specificity, change in binding energy, transformation pathway, and C-K production from ginsenosides Rc and C-Mc. The L213A variant ß-glycosidase catalyzed the conversion of Rc to Rd by hydrolyzing α-l-arabinofuranoside linked to Rc, whereas the wild-type ß-glycosidase did not. The variant enzyme converted ginsenosides Rc and C-Mc into C-K with molar conversions of 97%, which were 1.5- and 2-fold higher, respectively, than those of the wild-type enzyme. Therefore, protein engineering is a useful tool for enhancing the hydrolytic activity on specific glycoside linked to ginsenosides.
[Mh] Termos MeSH primário: Ginsenosídeos/metabolismo
Glicosídeo Hidrolases/metabolismo
Sulfolobus solfataricus/enzimologia
beta-Glucosidase/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Genes Bacterianos
Mutagênese Sítio-Dirigida
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
beta-Glucosidase/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ginsenosides); 0 (ginsenoside M1); 0K83B0L786 (ginsenoside Rc); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.55 (alpha-N-arabinofuranosidase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191018


  2 / 3877 MEDLINE  
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[PMID]:29338043
[Au] Autor:Almeida VM; Frutuoso MA; Marana SR
[Ad] Endereço:Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, SP, Brazil.
[Ti] Título:Search for independent (ß/α)4 subdomains in a (ß/α)8 barrel ß-glucosidase.
[So] Source:PLoS One;13(1):e0191282, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteins that fold as (ß/α)8 barrels are thought to have evolved from half-barrels that underwent duplication and fusion events. The evidence is particularly clear for small barrels, which have almost identical halves. Additionally, computational calculations of the thermodynamic stability of these structures in the presence of denaturants have revealed that (ß/α)8 barrels contain two subunits or domains corresponding to half-barrels. Hence, within (ß/α)8 barrels, half-barrels are self-contained units. Here, we tested this hypothesis using ß-glucosidase from the bacterium Thermotoga maritima (bglTm), which has a (ß/α)8 barrel structure. Mutations were introduced to disrupt the noncovalent contacts between its halves and reveal the presence of two domains within bglTm, thus resulting in the creation of mutants T1 (containing W12A and I217A mutations) and T2 (containing W12A, H195A, I217A and F404A mutations). Mutants T1 and T2 were properly folded, as indicated by their fluorescence spectra and enzyme kinetic parameters. T1 and wild-type bglTm were equally stable, as shown by the results of thermal inactivation, differential scanning fluorimetry and guanidine hydrochloride denaturation experiments. However, T2 showed a first-order inactivation at 80°C, a single melting temperature of 82°C and only one transition concentration (c50) in 2.4 M guanidine hydrochloride. Additionally, T1 and T2 exhibited a cooperative denaturation process that followed a two-state model (m-values equal to 1.4 and 1.6 kcal/mol/M, respectively), similar to that of wild-type bglTm (1.2 kcal/mol/M). Hence, T1 and T2 each denatured as a single unit, although they contained different degrees of disruption between their halves. In conclusion, bglTm halves are equivalent in terms of their thermal and chemical stability; thus, their separate contributions to (ß/α)8 barrel unfolding cannot be disentangled.
[Mh] Termos MeSH primário: beta-Glucosidase/química
beta-Glucosidase/metabolismo
[Mh] Termos MeSH secundário: Ativação Enzimática
Cinética
Modelos Moleculares
Mutação
Conformação Proteica em Folha beta
Domínios Proteicos
Temperatura Ambiente
Thermotoga maritima/enzimologia
beta-Glucosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.2.1.21 (beta-Glucosidase)
[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:180117
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191282


  3 / 3877 MEDLINE  
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[PMID]:29293326
[Au] Autor:Ide M; Okumura M; Koizumi K; Kumagai M; Yoshida I; Yoshida M; Mishima T; Nakamura M
[Ad] Endereço:Japan Food Research Laboratories , Osaka 567-0085, Japan.
[Ti] Título:Novel Method to Quantify ß-Glucan in Processed Foods: Sodium Hypochlorite Extracting and Enzymatic Digesting (SEED) Assay.
[So] Source:J Agric Food Chem;66(4):1033-1038, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Some ß-glucans have attracted attention due to their functionality as an immunostimulant and have been used in processed foods. However, accurately measuring the ß-glucan content of processed foods using existing methods is difficult. We demonstrate a new method, the Sodium hypochlorite Extracting and Enzymatic Digesting (SEED) assay, in which ß-glucan is extracted using sodium hypochlorite, dimethyl sulfoxide, and 5 mol/L sodium hydroxide and then digested into ß-glucan fragments using Westase which is an enzyme having ß-1,6- and ß-1,3 glucanase activity. The ß-glucan fragments are further digested into glucose using exo-1,3-ß-d-glucanase and ß-glucosidase. We measured ß-glucan comprising ß-1,3-, -1,6-, and -1,(3),4- bonds in various polysaccharide reagents and processed foods using our novel method. The SEED assay was able to quantify ß-glucan with good reproducibility, and the recovery rate was >90% for food containing ß-glucan. Therefore, the SEED assay is capable of accurately measuring the ß-glucan content of processed foods.
[Mh] Termos MeSH primário: Análise de Alimentos/métodos
Hipoclorito de Sódio
beta-Glucanas/análise
[Mh] Termos MeSH secundário: Manipulação de Alimentos
Glucana 1,3-beta-Glucosidase/metabolismo
Glucanos/química
Hordeum/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucans); 0 (beta-Glucans); 9008-22-4 (laminaran); DY38VHM5OD (Sodium Hypochlorite); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase); EC 3.2.1.58 (beta-1,3-exoglucanase)
[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:180103
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05044


  4 / 3877 MEDLINE  
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[PMID]:29239606
[Au] Autor:Fan L; Xie P; Wang Y; Huang Z; Zhou J
[Ad] Endereço:Institute of Agro-product Processing , Jiangsu Academy of Agricultural Sciences, Nanjing, Jiangsu 210014, China.
[Ti] Título:Biosurfactant-Protein Interaction: Influences of Mannosylerythritol Lipids-A on ß-Glucosidase.
[So] Source:J Agric Food Chem;66(1):238-246, 2018 Jan 10.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this work, the influences of a biosurfactant, mannosylerythritol lipids-A (MEL-A) toward ß-glucosidase activity and their molecular interactions were studied by using differential scanning calorimetry (DSC), circular dichroism spectroscopy (CD), isothermal titration calorimetry (ITC), and docking simulation. The enzyme inhibition kinetics data showed that MEL-A at a low concentration (< critical micelle concentration (CMC), 20.0 ± 5.0 µM) enhanced ß-glucosidase activity, whereas it inhibited the enzyme activity at higher concentrations more than 20.0 µM, followed by a decreased V and K of ß-glucosidase. The thermodynamics and structural data demonstrated that the midpoint temperature (T ) and unfolding enthalpy (ΔH) of ß-glucosidase was shifted to high values (76.6 °C, 126.3 J/g) in the presence of MEL-A, and the secondary structure changes of ß-glucosidase, including the increased α-helix, ß-turn, or random coil contents, and a decreased ß-sheet content were caused by MEL-A at a CMC concentration. The further ITC and docking simulations suggested the bindings of MEL-A toward ß-glucosidase were driven by weak hydrophobic interactions happened between the amino acid residues of ß-glucosidase and the fatty acid residues of MEL-A, in addition to hydrogen bonds between amino acids and hydroxyl in glycosyl residues of this biosurfactant.
[Mh] Termos MeSH primário: Glicolipídeos/química
Lipídeo A/química
Tensoativos/química
beta-Glucosidase/química
[Mh] Termos MeSH secundário: Interações Hidrofóbicas e Hidrofílicas
Cinética
Ligação Proteica
Estrutura Secundária de Proteína
Temperatura Ambiente
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycolipids); 0 (Lipid A); 0 (Surface-Active Agents); 0 (mannosylerythritol lipid); EC 3.2.1.21 (beta-Glucosidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04469


  5 / 3877 MEDLINE  
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[PMID]:29253000
[Au] Autor:Lin S; Wang S; Si Y; Yang W; Zhu S; Ni W
[Ad] Endereço:College of Environmental and Resource Sciences, Zhejiang University, Key Laboratory of Agricultural Resource and Environment of Zhejiang Province, Hangzhou, P. R. China.
[Ti] Título:Variations in eco-enzymatic stoichiometric and microbial characteristics in paddy soil as affected by long-term integrated organic-inorganic fertilization.
[So] Source:PLoS One;12(12):e0189908, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To investigate the effects of different nutrient management regimes on the soil chemical, eco-enzymatic stoichiometric and microbial characteristics, soil samples were collected from a 30-year, long-term field experiment with six plots growing rice. The results showed that as integrated fertilization increased, so did the concentrations of soil total or available nutrients and microbial biomass carbon (MBC). Our results also found enhanced soil basal respiration and cumulative carbon mineralization compared to chemical fertilization alone at the same nutrient doses. The activities of soil protease (Pro), ß-glucosidase (ßG), N-acetyl-glucosaminidase (NAG) and acid phosphatase (AP) from the integrated fertilization treatments were significantly higher than those of the treatments without organic manure, so did the activities of soil leucyl aminopeptidase (LAP) and urease (Ure) from the treatment with organic manure in addition to farmer practise fertilization (NPKM2). The stoichiometric ratios, expressed as lnßG/ln(NAG+LAP)/lnPro/lnUre/lnAP, ranged from 1:0.94:1.04:0.67:1.01 to 1:0.98:1.10:0.78:1.25, indicating that the acquisition of C, N and P changed consistently and synchronously under different nutrient management strategies. Integrated fertilization was more beneficial to the acquisition and utilization of soil organic carbon compared to low-molecular-weight organic nitrogen. We concluded that protease and urease should be considered in eco-enzymatic stoichiometric assessments for the hydrolysis of proteins, amino acids, carbohydrates and phosphomonoesters in soil, and integrated fertilization with chemical fertilizers and organic manure should be recommended as a preferable nutrient management system for intensive rice cultivation.
[Mh] Termos MeSH primário: Agricultura/métodos
Carbono/química
Fertilizantes
Microbiologia do Solo
Solo/química
[Mh] Termos MeSH secundário: Acetilglucosaminidase/metabolismo
Fosfatase Ácida/metabolismo
Aminopeptidases/metabolismo
Biomassa
China
Esterco
Nitrogênio/química
Oryza
Fósforo/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fertilizers); 0 (Manure); 0 (Soil); 27YLU75U4W (Phosphorus); 7440-44-0 (Carbon); EC 3.1.3.2 (Acid Phosphatase); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.52 (Acetylglucosaminidase); EC 3.4.11.- (Aminopeptidases); N762921K75 (Nitrogen)
[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.0189908


  6 / 3877 MEDLINE  
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[PMID]:29056105
[Au] Autor:Llopart EE; Cian RE; López-Oliva MME; Zuleta Á; Weisstaub A; Drago SR
[Ad] Endereço:1Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Facultad de Ingeniería Química,Instituto de Tecnología de Alimentos,Universidad Nacional del Litoral,Santiago del Estero 2829,Santa Fe,Argentina.
[Ti] Título:Colonic and systemic effects of extruded whole-grain sorghum consumption in growing Wistar rats.
[So] Source:Br J Nutr;118(8):589-597, 2017 Oct.
[Is] ISSN:1475-2662
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Colonic effects of extruded whole-grain sorghum diets were evaluated using a model of growing rats. In all, twenty-four male Wistar rats were fed control (C), extruded white sorghum (EWS) or red sorghum (ERS). Consumption of sorghum diets showed satiety properties, with reduction of caecal pH, and lower activity of ß-glucosidase and ß-glucuronidase enzymes. Decreased copper zinc superoxide dismutase and manganese superoxide dismutase and increased catalase and glutathione peroxidase levels were observed in colonic mucosa. The induction of antioxidant enzymes occurred through the activation of the nuclear factor erythroid 2-related factor 2 protein and its subsequent translocation into the nucleus. ERS was able to decrease the proliferation of proximal mucosa of colon, demonstrating a possible effect against colorectal tumourigenesis. EWS increased proliferation and also apoptosis, ensuring the re-establishment of homoeostasis of the colonic mucosa. No antioxidant systemic effect (serum or hepatic level) was observed. It is likely that despite the extrusion the low bioavailability of the phenolic compounds of sorghum diets caused them to exert mainly acute effects at the colon level. Extruded whole-grain sorghum is a good functional ingredient that might be promising in dietary prevention of intestinal diseases.
[Mh] Termos MeSH primário: Colo/metabolismo
Dieta
Sorghum/química
Grãos Integrais/química
[Mh] Termos MeSH secundário: Animais
Catalase/metabolismo
Modelos Animais de Doenças
Glucuronidase/metabolismo
Glutationa Peroxidase/metabolismo
Concentração de Íons de Hidrogênio
Enteropatias/prevenção & controle
Mucosa Intestinal/metabolismo
Masculino
Fator 2 Relacionado a NF-E2/genética
Fator 2 Relacionado a NF-E2/metabolismo
Ratos
Ratos Wistar
Saciação
Superóxido Dismutase/metabolismo
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NF-E2-Related Factor 2); 0 (Nfe2l2 protein, rat); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Superoxide Dismutase); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.31 (Glucuronidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171024
[St] Status:MEDLINE
[do] DOI:10.1017/S0007114517002513


  7 / 3877 MEDLINE  
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[PMID]:28884658
[Au] Autor:Li Y; Xu GT; Chang JP; Guo LM; Yang XQ; Piao CG
[Ad] Endereço:1​The Key Laboratory of State Forestry Administration on Forest Protection, Research Institute of Forest Ecology Environment and Protection, Chinese Academy of Forestry, Beijing 100091, PR China.
[Ti] Título:Sphingobacterium corticis sp. nov., isolated from bark of Populus × euramericana.
[So] Source:Int J Syst Evol Microbiol;67(10):3860-3864, 2017 Oct.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A Gram-stain negative, aerobic, non-motile bacterial strain, 23D10-4-9 , was isolated from symptomatic canker bark tissue of Populus × euramericana. The isolate grew between 4 and 35 °C, with optimal growth occurring at 25 °C. The species was positive for catalase and negative for oxidase activity. Nitrate was not reduced to nitrite. It showed activities toward ß-galactosidase and ß-glucosidase. Citrate was not utilized. Acid was produced from d-glucose. The major fatty acids were iso-C15 : 0, C16 : 1ω7c and iso-C17 : 0 3-OH. The main polar lipid profiles of the novel isolate included phosphatidylethanolamine, phospholipids and seven unknown lipids. The predominant menaquinone of the novel isolate was MK-7. The DNA G+C content was 40.6 mol%. 16S rRNA gene data revealed that the novel isolate shares the greatest sequence similarity with Sphingobacterium populi 7Y-4 (96.1 %). Based on phenotypic and genotypic characteristics, the isolate represents a novel species within the genus Sphingobacterium, for which the name Sphingobacteriumcorticis sp. nov. is proposed. The type strain is 23D10-4-9 (=CFCC 12640 =KCTC 42248 ).
[Mh] Termos MeSH primário: Filogenia
Casca de Planta/microbiologia
Populus/microbiologia
Sphingobacterium/classificação
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
China
DNA Bacteriano/genética
Ácidos Graxos/química
Fosfolipídeos/química
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Sphingobacterium/genética
Sphingobacterium/isolamento & purificação
Vitamina K 2/análogos & derivados
Vitamina K 2/química
beta-Galactosidase/metabolismo
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 8427BML8NY (vitamin MK 7); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.23 (beta-Galactosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002210


  8 / 3877 MEDLINE  
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[PMID]:28873987
[Au] Autor:Goswami S; Das S; Datta S
[Ad] Endereço:Protein Engineering Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Mohanpur 741246, India.
[Ti] Título:Understanding the role of residues around the active site tunnel towards generating a glucose-tolerant ß-glucosidase from Agrobacterium tumefaciens 5A.
[So] Source:Protein Eng Des Sel;30(7):523-530, 2017 Jul 01.
[Is] ISSN:1741-0134
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Most ß-glucosidases are subjected to inhibition by the final hydrolysis product glucose resulting in the accumulation of cellobiose and oligosaccharides. This accumulated cellobiose and oligosaccharides further inhibit the activities of endoglucanase and cellobiohydrolases, resulting in the inhibition of cellulose degradation and a more expensive biofuel. To elucidate the mechanism(s) of glucose tolerance, we designed and characterised six mutations of a moderately glucose-tolerant ß-glucosidase (H0HC94) from the mesophilic bacterium Agrobacterium tumefaciens 5A. The hydrophobicity and steric were varied across non-conserved residues in specific regions of the active site tunnel. In contrast to the uncompetitive inhibition of WT enzyme by glucose, C174V and H229S are competitively inhibited pointing towards a possible glucose-binding site in the protein at these positions. Increasing hydrophobicity at the +1 subsite and increasing hydrophobicity and steric at +2 subsites seemed to be critical for glucose tolerance for this BG. Additionally, in L178E, specific activity was 1.8 times higher on the natural substrate cellobiose while both W127F and L178E mutants showed an enhancement in thermostability. The kinetic stability of W127F, V176A, L178A and L178E also increased between 2- and 3-folds compared to WT. Our results indicate that while the structure between subsites +1 and +2 is critical for the glucose tolerance, the specific residues may not be identical across such enzymes.
[Mh] Termos MeSH primário: Agrobacterium tumefaciens/enzimologia
Glucose/química
beta-Glucosidase/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Celobiose/química
Celulose/química
Celulose 1,4-beta-Celobiosidase/química
Celulose 1,4-beta-Celobiosidase/genética
Hidrólise
Cinética
Especificidade por Substrato
beta-Glucosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
16462-44-5 (Cellobiose); 9004-34-6 (Cellulose); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.91 (Cellulose 1,4-beta-Cellobiosidase); IY9XDZ35W2 (Glucose)
[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/gzx039


  9 / 3877 MEDLINE  
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[PMID]:28787452
[Au] Autor:Goren S; Lugassi N; Stein O; Yeselson Y; Schaffer AA; David-Schwartz R; Granot D
[Ad] Endereço:Institute of Plant Sciences, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel.
[Ti] Título:Suppression of sucrose synthase affects auxin signaling and leaf morphology in tomato.
[So] Source:PLoS One;12(8):e0182334, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Metabolic enzymes have been found to play roles in plant development. Sucrose synthase (SUS) is one of the two enzyme families involved in sucrose cleavage in plants. In tomato, six SUS genes have been found. We generated transgenic tomato plants with RNAi suppression of SlSUS1, SlSUS3 and SlSUS4 genes. Independent transgenic lines with RNAi suppression of more than one SUS gene exhibited morphological effects on their cotyledons and leaf structure, but there were no significant effects on their carbohydrate levels, demonstrating that SUS has a developmental function, in addition to its metabolic function. Shoot apices of the transgenic lines showed elevated expression of JAGGED (JAG) and the auxin transporter PIN1. In a PIN1-GFP fusion reporter/SUS-RNAi hybrid, PIN1-GFP patterns were altered in developing leaves (as compared to control plants), indicating that SlSUS suppression alters auxin signaling. These results suggest possible roles for SUS in the regulation of plant growth and leaf morphology, in association with the auxin-signaling pathway.
[Mh] Termos MeSH primário: Glucosiltransferases/genética
Ácidos Indolacéticos/metabolismo
Lycopersicon esculentum/citologia
Lycopersicon esculentum/enzimologia
Folhas de Planta/anatomia & histologia
Interferência de RNA
Transdução de Sinais/genética
[Mh] Termos MeSH secundário: Regulação da Expressão Gênica de Plantas/genética
Glucosiltransferases/deficiência
Isoenzimas/deficiência
Isoenzimas/genética
Lycopersicon esculentum/genética
Lycopersicon esculentum/crescimento & desenvolvimento
Folhas de Planta/crescimento & desenvolvimento
Regiões Promotoras Genéticas/genética
beta-Glucosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Indoleacetic Acids); 0 (Isoenzymes); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.13 (sucrose synthase); EC 3.2.1.21 (beta-Glucosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182334


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[PMID]:28777990
[Au] Autor:Rocha-Martín J; Martinez-Bernal C; Pérez-Cobas Y; Reyes-Sosa FM; García BD
[Ad] Endereço:Department of Biotechnology, Abengoa Research, Campus Palmas Altas, C/ Energía Solar n° 1, 41014 Seville, Spain.
[Ti] Título:Additives enhancing enzymatic hydrolysis of lignocellulosic biomass.
[So] Source:Bioresour Technol;244(Pt 1):48-56, 2017 Nov.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Linked to the development of cellulolytic enzyme cocktails from Myceliophthora thermophila, we studied the effect of different additives on the enzymatic hydrolysis yield. The hydrolysis of pretreated corn stover (PCS), sugar cane straw (PSCS) and microcrystalline cellulose (Avicel) was performed under industrial conditions using high solid loadings, limited mixing, and low enzyme dosages. The addition of polyethylene glycol (PEG4000) allowed to increase the glucose yields by 10%, 7.5%, and 32%, respectively in the three materials. PEG4000 did not have significant effect on the stability of the main individual enzymes but increased beta-glucosidase and endoglucanase activity by 20% and 60% respectively. Moreover, the presence of PEG4000 accelerated cellulase-catalyzed hydrolysis reducing up to 25% the liquefaction time. However, a preliminary economical assessment concludes that even with these improvements, a lower contribution of PEG4000 to the 2G bioethanol production costs would be needed to reach commercial feasibility.
[Mh] Termos MeSH primário: Biomassa
[Mh] Termos MeSH secundário: Celulase
Celulose
Hidrólise
Lignina
beta-Glucosidase
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
11132-73-3 (lignocellulose); 9004-34-6 (Cellulose); 9005-53-2 (Lignin); EC 3.2.1.21 (beta-Glucosidase); 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:170805
[St] Status:MEDLINE



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