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Pesquisa : D08.811.277.450.420.200.550 [Categoria DeCS]
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[PMID]:27871388
[Au] Autor:Sermsathanaswadi J; Baramee S; Tachaapaikoon C; Pason P; Ratanakhanokchai K; Kosugi A
[Ad] Endereço:Department of Chemical Technology, Faculty of Science and Technology, Suan Dusit University, 295 Rajasrima Road, Dusit, Bangkok 10300, Thailand; Biological Resources and Post-harvest Division, Japan International Research Center for Agricultural Sciences (JIRCAS), 1-1 Ohwashi, Tsukuba, Ibaraki 305-8
[Ti] Título:The family 22 carbohydrate-binding module of bifunctional xylanase/ß-glucanase Xyn10E from Paenibacillus curdlanolyticus B-6 has an important role in lignocellulose degradation.
[So] Source:Enzyme Microb Technol;96:75-84, 2017 Jan.
[Is] ISSN:1879-0909
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A newly isolated endo-ß-1,4-xylanase (Xyn10E) from Paenibacillus curdlanolyticus B-6 has a modular structure consisting of a family 22 carbohydrate-binding module (CBM), a glycoside hydrolase (GH) family 10 catalytic domain, two fibronectin type III (Fn3) domains, and a family 3 CBM at the C-terminus. Intact Xyn10E (rXyn10E), CBM22-deleted Xyn10E (X-CBM3), CBM3-deleted Xyn10E (X-CBM22), and GH10 catalytic domain only (X-GH10) were expressed in Escherichia coli. rXyn10E showed bifunctional degradation activity toward xylan and ß-glucan and also degraded microcrystalline cellulose. Although X-CBM3 and X-GH10 had drastically reduced xylanase and ß-glucanase activities, X-CBM22 mostly retained these activities. Similar K values were obtained for rXyn10E and X-CBM3, but k and k /K values for X-CBM3 and X-GH10 were lower than those for rXyn10E, suggesting that CBM22 of Xyn10E may contribute to catalytic efficiency. In binding assays, X-CBM3 was still able to bind to ß-glucan, soluble xylan, insoluble xylan, and cellulose through GH10 and CBM3. These results indicate that CBM22 has an important role not only in binding to xylan and ß-glucan but also in feeding both polysaccharides into the neighboring GH10 catalytic domain. rXyn10E showed remarkable synergism with rXyn11A, a major xylanase subunit of P. curdlanolyticus B-6, in the degradation of untreated corn stover and sugarcane bagasse; however, the combination of X-CBM3 and rXyn11A was not synergistic. These results indicate that Xyn10E and Xyn11A act synergistically on lignocellulosic biomass, and CBM22 is essential for efficient degradation of lignocellulosic materials.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Endo-1,4-beta-Xilanases/química
Endo-1,4-beta-Xilanases/metabolismo
Glucana 1,4-beta-Glucosidase/química
Glucana 1,4-beta-Glucosidase/metabolismo
Lignina/metabolismo
Paenibacillus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Domínio Catalítico
Endo-1,4-beta-Xilanases/genética
Genes Bacterianos
Glucana 1,4-beta-Glucosidase/genética
Cinética
Paenibacillus/genética
Filogenia
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia Estrutural de Proteína
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 11132-73-3 (lignocellulose); 9005-53-2 (Lignin); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase); EC 3.2.1.8 (Endo-1,4-beta Xylanases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170530
[Lr] Data última revisão:
170530
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161123
[St] Status:MEDLINE


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[PMID]:27780955
[Au] Autor:Jeong WS; Seo DH; Jung JH; Jung DH; Lee DW; Park YS; Park C
[Ad] Endereço:Graduate School of Biotechnology and Institute of Life Sciences & Resources, Kyung Hee University, Yongin 17104, Republic of Korea.
[Ti] Título:Enzymatic Characteristics of a Highly Thermostable ß-(1-4)-Glucanase from AW-1 (KCTC 4680).
[So] Source:J Microbiol Biotechnol;27(2):271-276, 2017 Feb 28.
[Is] ISSN:1738-8872
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:A highly thermostable ß-(1-4)-glucanase (NA23_08975) gene ( ) from AW-1, a native-feather degrading thermophilic eubacterium, was cloned and expressed in . The recombinant FiG (rFiG) protein showed strong activity toward ß- -glucan from barley (367.0 IU/mg), galactomannan (174.0 IU/mg), and 4-nitrophenyl-cellobioside (66.1 IU/mg), but relatively weak activity was observed with hydroxyethyl cellulose (5.3 IU/mg), carboxymethyl cellulose (2.4 IU/mg), and xylan from oat spelt (1.4 IU/mg). rFiG exhibited optimal activity at 90°C and pH 5.0. In addition, this enzyme was extremely thermostable, showing a half-life of 113 h at 85°C. These results indicate that rFiG could be used for hydrolysis of cellulosic and hemicellulosic biomass substrates for biofuel production.
[Mh] Termos MeSH primário: Bactérias Anaeróbias/enzimologia
Extremófilos/enzimologia
Glucana 1,4-beta-Glucosidase/química
Glucana 1,4-beta-Glucosidase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bactérias Anaeróbias/genética
Biocombustíveis
Celulose/metabolismo
Clonagem Molecular
Estabilidade Enzimática
Escherichia coli/genética
Escherichia coli/metabolismo
Glucana 1,4-beta-Glucosidase/genética
Glucana 1,4-beta-Glucosidase/isolamento & purificação
Concentração de Íons de Hidrogênio
Cinética
Mananas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Temperatura Ambiente
Xilanos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biofuels); 0 (Mannans); 0 (Recombinant Proteins); 0 (Xylans); 11078-30-1 (galactomannan); 9004-34-6 (Cellulose); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170328
[Lr] Data última revisão:
170328
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161027
[St] Status:MEDLINE
[do] DOI:10.4014/jmb.1609.09022


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[PMID]:26727898
[Au] Autor:Deng YJ; Wang SY
[Ad] Endereço:Department of Biological Sciences, The University of Southern Mississippi, 118 College Dr. # 5018, Hattiesburg, MS, 39406, USA.
[Ti] Título:Synergistic growth in bacteria depends on substrate complexity.
[So] Source:J Microbiol;54(1):23-30, 2016 Jan.
[Is] ISSN:1976-3794
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:Both positive and negative interactions among bacteria take place in the environment. We hypothesize that the complexity of the substrate affects the way bacteria interact with greater cooperation in the presence of recalcitrant substrate. We isolated lignocellulolytic bacteria from salt marsh detritus and compared the growth, metabolic activity and enzyme production of pure cultures to those of three-species mixed cultures in lignocellulose and glucose media. Synergistic growth was common in lignocellulose medium containing carboxyl methyl cellulose, xylan and lignin but absent in glucose medium. Bacterial synergism promoted metabolic activity in synergistic mixed cultures but not the maximal growth rate (µ). Bacterial synergism also promoted the production of ß-1,4-glucosidase but not the production of cellobiohydrolase or ß-1,4-xylosidase. Our results suggest that the chemical complexity of the substrate affects the way bacteria interact. While a complex substrate such as lignocellulose promotes positive interactions and synergistic growth, a labile substrate such as glucose promotes negative interactions and competition. Synergistic interactions among indigenous bacteria are suggested to be important in promoting lignocellulose degradation in the environment.
[Mh] Termos MeSH primário: Bactérias/crescimento & desenvolvimento
Lignina/metabolismo
Zonas Úmidas
[Mh] Termos MeSH secundário: Bactérias/classificação
Bactérias/isolamento & purificação
Bactérias/metabolismo
Celulose 1,4-beta-Celobiosidase/metabolismo
Meios de Cultura
Glucana 1,4-beta-Glucosidase/metabolismo
Glucose/metabolismo
Interações Microbianas
Xilosidases/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 (Culture Media); 11132-73-3 (lignocellulose); 9005-53-2 (Lignin); EC 3.2.1.- (Xylosidases); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase); EC 3.2.1.91 (Cellulose 1,4-beta-Cellobiosidase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160106
[St] Status:MEDLINE
[do] DOI:10.1007/s12275-016-5461-9


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[PMID]:26566837
[Au] Autor:Minoia S; Boualem A; Marcel F; Troadec C; Quemener B; Cellini F; Petrozza A; Vigouroux J; Lahaye M; Carriero F; Bendahmane A
[Ad] Endereço:INRA, UMR1403, IPS2, CNRS-UMR 9213, Université Paris-Sud, Université d'Evry, Université Paris-Diderot, Sorbonne Paris-Cité, 2 rue Gaston Crémieux, 91057 Evry, France; ALSIA, Centro Ricerche Metapontum Agrobios, SS Jonica 106 Km 448.2, 75012 Metaponto (MT), Italy. Electronic address: sminoia@hotmail.
[Ti] Título:Induced mutations in tomato SlExp1 alter cell wall metabolism and delay fruit softening.
[So] Source:Plant Sci;242:195-202, 2016 Jan.
[Is] ISSN:1873-2259
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Fruit ripening and softening are key traits for many fleshy fruit. Since cell walls play a key role in the softening process, expansins have been investigated to control fruit over ripening and deterioration. In tomato, expression of Expansin 1 gene, SlExp1, during fruit ripening was associated with fruit softening. To engineer tomato plants with long shelf life, we screened for mutant plants impaired in SlExp1 function. Characterization of two induced mutations, Slexp1-6_W211S, and Slexp1-7_Q213Stop, showed that SlExp1 loss of function leads to enhanced fruit firmness and delayed fruit ripening. Analysis of cell wall polysaccharide composition of Slexp1-7_Q213Stop mutant pointed out significant differences for uronic acid, neutral sugar and total sugar contents. Hemicelluloses chemistry analysis by endo-ß-1,4-d-glucanase hydrolysis and MALDI-TOF spectrometry revealed that xyloglucan structures were affected in the fruit pericarp of Slexp1-7_Q213Stop mutant. Altogether, these results demonstrated that SlExp1 loss of function mutants yield firmer and late ripening fruits through modification of hemicellulose structure. These SlExp1 mutants represent good tools for breeding long shelf life tomato lines with contrasted fruit texture as well as for the understanding of the cell wall polysaccharide assembly dynamics in fleshy fruits.
[Mh] Termos MeSH primário: Parede Celular/genética
Frutas/genética
Lycopersicon esculentum/genética
Mutação
Proteínas de Plantas/genética
[Mh] Termos MeSH secundário: Parede Celular/metabolismo
Cristalografia por Raios X
Frutas/metabolismo
Frutas/fisiologia
Glucana 1,4-beta-Glucosidase/metabolismo
Glucanos/metabolismo
Lycopersicon esculentum/metabolismo
Lycopersicon esculentum/fisiologia
Modelos Moleculares
Mutagênese
Proteínas de Plantas/química
Proteínas de Plantas/metabolismo
Polissacarídeos/metabolismo
Estrutura Terciária de Proteína
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Fatores de Tempo
Ácidos Urônicos/metabolismo
Xilanos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glucans); 0 (Plant Proteins); 0 (Polysaccharides); 0 (Uronic Acids); 0 (Xylans); 37294-28-3 (xyloglucan); 8024-50-8 (hemicellulose); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151115
[St] Status:MEDLINE


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[PMID]:25535714
[Au] Autor:Singh MP; Pandey AK; Vishwakarma SK; Srivastava AK; Pandey VK; Singh VK
[Ad] Endereço:University of Allahabad Centre of Biotechnology Allahabad India mpsingh.16@gmail.com.
[Ti] Título:Production of cellulolytic enzymes by Pleurotus species on lignocellulosic wastes using novel pretreatments.
[So] Source:Cell Mol Biol (Noisy-le-grand);60(5):59-63, 2014 Dec 24.
[Is] ISSN:1165-158X
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:In the present investigation three species of Pleurotus i.e. P. sajor—caju (P1), P. florida (P2) and P. flabellatus (P3) along with two lignocellulosic substrates namely paddy straw and wheat straw were selected for evaluation of production of extracellular cellulolytic enzymes. During the cultivation of three species of Pleurotus under in vivo condition, the two lignocellulosic substrates were treated with plants extracts (aqueous extracts of ashoka leaves (A) and neem oil (B)), hot water (H) and chemicals (C).Among all treatments, neem oil treated substrates supported better enzyme production followed by aqueous extract of ashoka leaves, hot water and chemical treatment. Between the two substrates paddy straw supported better enzyme production than wheat straw. P. flabellatus showed maximum activity of exoglucanase, endoglucanase and β—glucosidase followed by P. florida and P. sajor—caju.
[Mh] Termos MeSH primário: Lignina/metabolismo
Pleurotus/enzimologia
[Mh] Termos MeSH secundário: Biodegradação Ambiental
Celulase/metabolismo
Glucana 1,4-beta-Glucosidase/metabolismo
Pleurotus/metabolismo
Eliminação de Resíduos/métodos
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
11132-73-3 (lignocellulose); 9005-53-2 (Lignin); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.4 (Cellulase); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:141224
[Lr] Data última revisão:
141224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141224
[St] Status:MEDLINE


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[PMID]:24667929
[Au] Autor:Zhang X; Wang W; Chen W; Zhang N; Zeng H
[Ad] Endereço:Department of Ecology, College of Urban and Environmental Sciences and the Key Laboratory for Earth Surface Processes of the Ministry of Education, Peking University, Beijing, China; Key Laboratory for Cyclic Economy, School of Urban Planning and Design, Shenzhen Graduate School, Peking University,
[Ti] Título:Comparison of seasonal soil microbial process in snow-covered temperate ecosystems of northern China.
[So] Source:PLoS One;9(3):e92985, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:More than half of the earth's terrestrial surface currently experiences seasonal snow cover and soil frost. Winter compositional and functional investigations in soil microbial community are frequently conducted in alpine tundra and boreal forest ecosystems. However, little information on winter microbial biogeochemistry is known from seasonally snow-covered temperate ecosystems. As decomposer microbes may differ in their ability/strategy to efficiently use soil organic carbon (SOC) within different phases of the year, understanding seasonal microbial process will increase our knowledge of biogeochemical cycling from the aspect of decomposition rates and corresponding nutrient dynamics. In this study, we measured soil microbial biomass, community composition and potential SOC mineralization rates in winter and summer, from six temperate ecosystems in northern China. Our results showed a clear pattern of increased microbial biomass C to nitrogen (N) ratio in most winter soils. Concurrently, a shift in soil microbial community composition occurred with higher fungal to bacterial biomass ratio and gram negative (G-) to gram positive (G+) bacterial biomass ratio in winter than in summer. Furthermore, potential SOC mineralization rate was higher in winter than in summer. Our study demonstrated a distinct transition of microbial community structure and function from winter to summer in temperate snow-covered ecosystems. Microbial N immobilization in winter may not be the major contributor for plant growth in the following spring.
[Mh] Termos MeSH primário: Ecossistema
Estações do Ano
Neve
Microbiologia do Solo
Solo
[Mh] Termos MeSH secundário: Bactérias/isolamento & purificação
Bactérias/metabolismo
Biomassa
Carbono/metabolismo
China
Fungos/isolamento & purificação
Fungos/metabolismo
Glucana 1,4-beta-Glucosidase/metabolismo
Minerais/metabolismo
Nitrogênio/metabolismo
Fosfolipídeos/metabolismo
Fenômenos Físicos
Solo/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Minerals); 0 (Phospholipids); 0 (Soil); 7440-44-0 (Carbon); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase); N762921K75 (Nitrogen)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140327
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0092985


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[PMID]:24146430
[Au] Autor:Chahed H; Ezzine A; Mlouka AB; Hardouin J; Jouenne T; Marzouki MN
[Ad] Endereço:Laboratoire d'Ingénierie des Protéines et des Molécules Bioactives (LIP-MB), National Institute of Applied Sciences and Technology, University of Carthage, 1080, Tunis Cedex, Tunisia.
[Ti] Título:Biochemical characterization, molecular cloning, and structural modeling of an interesting ß-1,4-glucanase from Sclerotinia sclerotiorum.
[So] Source:Mol Biotechnol;56(4):340-50, 2014 Apr.
[Is] ISSN:1559-0305
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The filamentous fungus Sclerotinia sclerotiorum produces a complete set of cellulolytic enzymes needed for efficient solubilization of native cellulose, the major component of plants. In this work, we reported the molecular characterization of an important glycosyl-hydrolase enzyme classified as endo-ß-1,4-glucanase. The importance of this enzyme was revealed with the in-gel activity staining, showing a high degradation capacity of cellulose. When purified from native gel and ran in denaturing polyacrylamide gel, the polypeptide has an apparent molecular mass of about 34 kDa called Endo2. For further characterization of this protein, a mass spectrometry approach was carried out. The LC-MS/MS analysis revealed two peptides belonging to this enzyme. The genomic DNA and cDNA sequences were resolved by PCR amplification and sequencing, revealing a gene with two intron sequences. The open reading frame of 987 bp encoded a putative polypeptide of 328 amino acids having a calculated molecular mass of 33,297 Da. Yet, the molecular modeling and comparative investigation of different 3D cellulase structures showed that this endoglucanase isoform has probably two domains. A core domain having a high similarity with endoglucanases family 5 and a cellulose-binding domain having similarities with those of exo-type cellulases of family 1, linked together by a serine-threonine-rich region. These results are with great interests and show new characteristics of S. sclerotiorum glucanase.
[Mh] Termos MeSH primário: Ascomicetos/enzimologia
Glucana 1,4-beta-Glucosidase/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Ascomicetos/genética
Glucana 1,4-beta-Glucosidase/biossíntese
Glucana 1,4-beta-Glucosidase/química
Conformação Proteica
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131023
[St] Status:MEDLINE
[do] DOI:10.1007/s12033-013-9714-0


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[PMID]:22904050
[Au] Autor:Adlakha N; Sawant S; Anil A; Lali A; Yazdani SS
[Ad] Endereço:Synthetic Biology and Biofuel Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi, India.
[Ti] Título:Specific fusion of ß-1,4-endoglucanase and ß-1,4-glucosidase enhances cellulolytic activity and helps in channeling of intermediates.
[So] Source:Appl Environ Microbiol;78(20):7447-54, 2012 Oct.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Identification and design of new cellulolytic enzymes with higher catalytic efficiency are a key factor in reducing the production cost of lignocellulosic bioalcohol. We report here identification of a novel ß-glucosidase (Gluc1C) from Paenibacillus sp. strain MTCC 5639 and construction of bifunctional chimeric proteins based on Gluc1C and Endo5A, a ß-1,4-endoglucanase isolated from MTCC 5639 earlier. The 448-amino-acid-long Gluc1C contained a GH superfamily 1 domain and hydrolyzed cellodextrin up to a five-sugar chain length, with highest efficiency toward cellobiose. Addition of Gluc1C improved the ability of Endo5A to release the reducing sugars from carboxymethyl cellulose. We therefore constructed six bifunctional chimeric proteins based on Endo5A and Gluc1C varying in the positions and sizes of linkers. One of the constructs, EG5, consisting of Endo5A-(G(4)S)(3)-Gluc1C, demonstrated 3.2- and 2-fold higher molar specific activities for ß-glucosidase and endoglucanase, respectively, than Gluc1C and Endo5A alone. EG5 also showed 2-fold higher catalytic efficiency than individual recombinant enzymes. The thermal denaturation monitored by circular dichroism (CD) spectroscopy demonstrated that the fusion of Gluc1C with Endo5A resulted in increased thermostability of both domains by 5°C and 9°C, respectively. Comparative hydrolysis experiments done on alkali-treated rice straw and CMC indicated 2-fold higher release of product by EG5 than that by the physical mixture of Endo5A and Gluc1C, providing a rationale for channeling of intermediates. Addition of EG5 to a commercial enzyme preparation significantly enhanced release of reducing sugars from pretreated biomass, indicating its commercial applicability.
[Mh] Termos MeSH primário: Carboximetilcelulose Sódica/metabolismo
Celulase/genética
Celulase/metabolismo
Glucana 1,4-beta-Glucosidase/genética
Glucana 1,4-beta-Glucosidase/metabolismo
Paenibacillus/enzimologia
[Mh] Termos MeSH secundário: Dicroísmo Circular
Estabilidade Enzimática
Hidrólise
Oryza/metabolismo
Paenibacillus/genética
Conformação Proteica/efeitos da radiação
Estabilidade Proteica
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Recombinant Fusion Proteins); EC 3.2.1.4 (Cellulase); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase); K679OBS311 (Carboxymethylcellulose Sodium)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120821
[St] Status:MEDLINE


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[PMID]:22714267
[Au] Autor:Haq IU; Khan MA; Muneer B; Hussain Z; Afzal S; Majeed S; Rashid N; Javed MM; Ahmad I
[Ad] Endereço:Institute of Industrial Biotechnology, GC University, Lahore 54000, Pakistan. chemistrymak@yahoo.com
[Ti] Título:Cloning, characterization and molecular docking of a highly thermostable ß-1,4-glucosidase from Thermotoga petrophila.
[So] Source:Biotechnol Lett;34(9):1703-9, 2012 Sep.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A genomic DNA fragment, encoding a thermotolerant ß-glucosidase, of the obligate anaerobe Thermotoga petrophila RKU-1 was cloned after PCR amplification into Escherichia coli strain BL21 CodonPlus. The purified cloned enzyme was a monomeric, 51.5 kDa protein (by SDS-PAGE) encoded by 1.341 kb gene. The estimated K (m) and V (max) values against p-nitrophenyl-ß-D-glucopyranoside were 2.8 mM and 42.7 mmol min(-1) mg(-1), respectively. The enzyme was also active against other p-nitrophenyl substrates. Possible catalytic sites involved in hydrolyzing different p-nitrophenyl substrates are proposed based on docking studies of enzyme with its substrates. Because of its unique characters, this enzyme is a potential candidate for industrial applications.
[Mh] Termos MeSH primário: Bactérias Anaeróbias/enzimologia
Glucana 1,4-beta-Glucosidase/genética
Glucana 1,4-beta-Glucosidase/metabolismo
[Mh] Termos MeSH secundário: Bactérias Anaeróbias/genética
Clonagem Molecular
Eletroforese em Gel de Poliacrilamida
Escherichia coli/genética
Glucana 1,4-beta-Glucosidase/química
Glucana 1,4-beta-Glucosidase/isolamento & purificação
Glucosídeos/metabolismo
Hidrólise
Cinética
Modelos Moleculares
Simulação de Dinâmica Molecular
Peso Molecular
Reação em Cadeia da Polimerase
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glucosides); 0 (Recombinant Proteins); 2492-87-7 (4-nitrophenyl beta-D-glucoside); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase)
[Em] Mês de entrada:1301
[Cu] Atualização por classe:120831
[Lr] Data última revisão:
120831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120621
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-012-0953-0


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[PMID]:22129429
[Au] Autor:Nakatani Y; Cutfield SM; Cowieson NP; Cutfield JF
[Ad] Endereço:Department of Biochemistry, University of Otago, Dunedin, New Zealand.
[Ti] Título:Structure and activity of exo-1,3/1,4-ß-glucanase from marine bacterium Pseudoalteromonas sp. BB1 showing a novel C-terminal domain.
[So] Source:FEBS J;279(3):464-78, 2012 Feb.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Following the discovery of an exo-1,3/1,4-ß-glucanase (glycoside hydrolase family 3) from a seaweed-associated bacterium Pseudoalteromonas sp. BB1, the recombinant three-domain protein (ExoP) was crystallized and its structure solved to 2.3 Å resolution. The first two domains of ExoP, both of which contribute to the architecture of the active site, are similar to those of the two-domain barley homologue ß-d-glucan exohydrolase (ExoI) with a distinctive Trp-Trp clamp at the +1 subsite, although ExoI displays broader specificity towards ß-glycosidic linkages. Notably, excision of the third domain of ExoP results in an inactive enzyme. Domain 3 has a ß-sandwich structure and was shown by CD to be more temperature stable than the native enzyme. It makes relatively few contacts to domain 1 and none at all to domain 2. Two of the domain 3 residues involved at the interface, Q683 (forming one hydrogen bond) and Q676 (forming two hydrogen bonds) were mutated to alanine. Variant Q676A retained about half the activity of native ExoP, but the Q683A variant was severely attenuated. The crystal structure of Q683A-ExoP indicated that domain 3 was highly mobile and that Q683 is critical to the stabilization of ExoP by domain 3. Small-angle X-ray scattering data lent support to this proposal. Domain 3 does not appear to be an obvious carbohydrate-binding domain and is related neither in sequence nor structure to the additional domains characterized in other glycoside hydrolase 3 subgroups. Its major role appears to be for protein stability but it may also help orient substrate. DATABASE: Structural data are available in the Protein Data Bank under the accession numbers 3UT0, 3USZ, 3F95 and 3RRX.
[Mh] Termos MeSH primário: Glucana 1,3-beta-Glucosidase/química
Glucana 1,4-beta-Glucosidase/química
Pseudoalteromonas/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cristalografia por Raios X
Estabilidade Enzimática
Glucana 1,3-beta-Glucosidase/metabolismo
Glucana 1,4-beta-Glucosidase/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
Estrutura Quaternária de Proteína
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase); EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase)
[Em] Mês de entrada:1204
[Cu] Atualização por classe:130520
[Lr] Data última revisão:
130520
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111202
[St] Status:MEDLINE
[do] DOI:10.1111/j.1742-4658.2011.08439.x



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