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Pesquisa : D08.811.277.450.420.200.450 [Categoria DeCS]
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  1 / 99 MEDLINE  
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[PMID]:28551269
[Au] Autor:Zhang B; Liu Y; Yang H; Yan Q; Yang S; Jiang ZQ; Li S
[Ad] Endereço:College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471023, China; Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
[Ti] Título:Biochemical properties and application of a novel ß-1,3-1,4-glucanase from Paenibacillus barengoltzii.
[So] Source:Food Chem;234:68-75, 2017 Nov 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel endo-ß-1,3-1,4-glucanase gene (PbBglu16A) was cloned from Paenibacillus barengoltzii and heterogeneously expressed in Escherichia coli. The recombinant ß-1,3-1,4-glucanase (PbBglu16A) was purified to homogeneity with a recovery yield of 78.6% and a specific activity of 431.8Umg . The molecular mass of PbBglu16A was estimated to be 44.0kDa by SDS-PAGE. The optimal pH and temperature of PbBglu16A were 6.0 and 55°C, respectively. The enzyme was stable within pH 3.5-9.0 and up to 55°C. PbBglu16A exhibited high substrate specificity towards barley ß-glucan, oat ß-glucan and lichenin. PbBglu16A showed an endo-type cleavage pattern and hydrolyzed endogenous enzyme-deactivated oat bran into ß-gluco-oligosaccharides with a yield of 7.0%, which mainly consisted of trioligosaccharide and tetraoligosaccharide. Further, PbBglu16A could promote mashing with a reduced filtration time (14.0%) and viscosity (3.4%). Thus, PbBglu16A might be a promising candidate for the production of ß-gluco-oligosaccharides and in brewing industry.
[Mh] Termos MeSH primário: Endo-1,3(4)-beta-Glucanase/química
Paenibacillus/enzimologia
beta-Glucanas/metabolismo
[Mh] Termos MeSH secundário: Clonagem Molecular
Eletroforese em Gel de Poliacrilamida
Estabilidade Enzimática
Escherichia coli
Concentração de Íons de Hidrogênio
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-Glucans); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE


  2 / 99 MEDLINE  
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[PMID]:28126846
[Au] Autor:Ji R; Ye W; Chen H; Zeng J; Li H; Yu H; Li J; Lou Y
[Ad] Endereço:State Key Laboratory of Rice Biology, Institute of Insect Science, Zhejiang University, Hangzhou 310058, Zhejiang, China.
[Ti] Título:A Salivary Endo-ß-1,4-Glucanase Acts as an Effector That Enables the Brown Planthopper to Feed on Rice.
[So] Source:Plant Physiol;173(3):1920-1932, 2017 Mar.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The brown planthopper (BPH) is one of the most destructive insect pests on rice ( ) in Asia. After landing on plants, BPH rapidly accesses plant phloem and sucks the phloem sap through unknown mechanisms. We discovered a salivary endo-ß-1,4-glucanase (NlEG1) that has endoglucanase activity with a maximal activity at pH 6 at 37°C and is secreted into rice plants by BPH is highly expressed in the salivary glands and midgut. Silencing decreases the capacity of BPH to reach the phloem and reduces its food intake, mass, survival, and fecundity on rice plants. By contrast, silencing had only a small effect on the survival rate of BPH raised on artificial diet. Moreover, NlEG1 secreted by BPH did not elicit the production of the defense-related signal molecules salicylic acid, jasmonic acid, and jasmonoyl-isoleucine in rice, although wounding plus the application of the recombination protein NlEG1 did slightly enhance the levels of jasmonic acid and jasmonoyl-isoleucine in plants compared with the corresponding controls. These data suggest that NlEG1 enables the BPH's stylet to reach the phloem by degrading celluloses in plant cell walls, thereby functioning as an effector that overcomes the plant cell wall defense in rice.
[Mh] Termos MeSH primário: Endo-1,3(4)-beta-Glucanase/metabolismo
Comportamento Alimentar/fisiologia
Hemípteros/fisiologia
Proteínas de Insetos/metabolismo
Oryza/parasitologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Parede Celular/metabolismo
Celulose/metabolismo
Ciclopentanos/metabolismo
Endo-1,3(4)-beta-Glucanase/classificação
Endo-1,3(4)-beta-Glucanase/genética
Fertilidade/genética
Regulação Enzimológica da Expressão Gênica
Hemípteros/enzimologia
Hemípteros/genética
Interações Hospedeiro-Parasita
Proteínas de Insetos/classificação
Proteínas de Insetos/genética
Oxilipinas/metabolismo
Floema/parasitologia
Filogenia
Interferência de RNA
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Saliva/enzimologia
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclopentanes); 0 (Insect Proteins); 0 (Oxylipins); 6RI5N05OWW (jasmonic acid); 9004-34-6 (Cellulose); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase)
[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:170128
[St] Status:MEDLINE
[do] DOI:10.1104/pp.16.01493


  3 / 99 MEDLINE  
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[PMID]:28007217
[Au] Autor:Wang J; Kang L; Liu Z; Yuan S
[Ad] Endereço:Jiangsu Key Laboratory for Microbes and Microbial Functional Genomics, Jiangsu Engineering and Technology Research Center for Industrialization of Microbial Resources, College of Life Science, Nanjing Normal University, Nanjing 210023, PR China.
[Ti] Título:Gene cloning, heterologous expression and characterization of a Coprinopsis cinerea endo-ß-1,3(4)-glucanase.
[So] Source:Fungal Biol;121(1):61-68, 2017 Jan.
[Is] ISSN:1878-6146
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A gene coding endo-ß-1,3(4)-glucanase (ENG16A) was cloned from Coprinopsis cinerea and heterologously expressed in Pichia pastoris. ENG16A only acts on substrates containing ß-1,3 glycosidic bonds but not on substrates containing only ß-1,4- or ß-1,6-glycosidic bonds. Interestingly, compared to the activity of this enzyme towards carboxymethyl (CM)-pachyman containing only ß-1,3-glycosidic bonds, its activity towards barley ß-glucan containing both ß-1,3-glycosidic and ß-1,4-glycosidic bonds was increased by 64.72 %,, its activity towards laminarin containing both ß-1,3-glycosidic and ß-1,6-glycosidic bonds was decreased by 50.83 %. In addition, ENG16A has a higher Km value and Vmax for barley ß-glucan than laminarin, which may be related to the fact that barley ß-glucan contains mainly ß-1,4-glycosidic bonds mixed with a few ß-1,3-glycosidic bonds, whereas laminarin mainly contains ß-1,3-glycosidic bonds with a few ß-1,6-branched glucose residues. The adjacent ß-1,4-glycosidic bond promotes ENG16A to hydrolyse ß-1,3-glycosidic bonds, leading to an increased Vmax; the nearby ß-1,6-glycosidic bonds inhibited its hydrolysis of ß-1,3-glycosidic bonds, resulting in a decreased Vmax. This property is suggested to be related to the mechanism that C. cinerea uses to degrade and utilize hemicellulose in straw medium and to protect its cell wall during the mycelium growth stage.
[Mh] Termos MeSH primário: Agaricales/enzimologia
Endo-1,3(4)-beta-Glucanase/metabolismo
[Mh] Termos MeSH secundário: Agaricales/genética
Clonagem Molecular
Endo-1,3(4)-beta-Glucanase/química
Endo-1,3(4)-beta-Glucanase/genética
Expressão Gênica
Pichia/genética
Pichia/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161224
[St] Status:MEDLINE


  4 / 99 MEDLINE  
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[PMID]:27765566
[Au] Autor:Lee JM; Moon SY; Kim YR; Kim KW; Lee BJ; Kong IS
[Ad] Endereço:Department of Biotechnology, Pukyong National University, Busan, 608-737, Republic of Korea.
[Ti] Título:Improvement of thermostability and halostability of ß-1,3-1,4-glucanase by substituting hydrophobic residue for Lys .
[So] Source:Int J Biol Macromol;94(Pt A):594-602, 2017 Jan.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The aim of this study was to improve the stability of ß-1,3-1,4-glucanase by substituting hydrophobic residue for specific amino acid. The results indicated that the catalytic efficiency, thermostability and halostability were enhanced simultaneously by replacement of Lys48 with Ala (K48A) or Leu (K48L). Comparison of kinetic parameters revealed that catalytic efficiency of mutants is enhanced as a result of the increase in substrate affinity. A great improvement in thermostability and halostability was observed. The half-lives of mutants significantly increased (up to ∼7-fold) at 60-70°C. Moreover, relative enzymatic activities of mutants were observed more than 80% even in the presence of 30% NaCl, and half-lives were increased to 3-fold that of wild-type. Based on above results, when applied to ionic liquid, mutants were more active and stable compared to wild-type. These were the results from improvement of protein functions by the substitution of hydrophobic single residue in adjacent with forming carbohydrate binding cavity. Therefore, this report could be helpful for improvement of the enzyme property and for biotechnological application as well.
[Mh] Termos MeSH primário: Alanina/química
Bacillus/química
Proteínas de Bactérias/química
Endo-1,3(4)-beta-Glucanase/química
Leucina/química
Lisina/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Bacillus/enzimologia
Proteínas de Bactérias/genética
Biocatálise
Endo-1,3(4)-beta-Glucanase/genética
Estabilidade Enzimática
Temperatura Alta
Interações Hidrofóbicas e Hidrofílicas
Líquidos Iônicos/química
Cinética
Mutagênese Sítio-Dirigida
Mutação
Alinhamento de Sequência
Cloreto de Sódio/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Ionic Liquids); 451W47IQ8X (Sodium Chloride); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase); GMW67QNF9C (Leucine); K3Z4F929H6 (Lysine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161030
[St] Status:MEDLINE


  5 / 99 MEDLINE  
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[PMID]:26611612
[Au] Autor:Li J; Xu X; Shi P; Liu B; Zhang Y; Zhang W
[Ad] Endereço:Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, PR China.
[Ti] Título:Overexpression and characterization of a novel endo-ß-1,3(4)-glucanase from thermophilic fungus Humicola insolens Y1.
[So] Source:Protein Expr Purif;138:63-68, 2017 Oct.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A novel endo-ß-1,3(4)-glucanase gene, cel16A, was cloned from the fungus Humicola insolens Y1. The 988-bp full-length gene encoded a 286-residue polypeptide consisting of a putative signal peptide of 20 residues and a catalytic domain belonging to glycosyl hydrolase family 16. It was successfully overexpressed in Pichia pastoris GS115. The purified recombinant Cel16A exhibited highest specific activity toward barley ß-glucan, followed by lichenan and laminarin, but not toward CMC-Na, birchwood xylan, Avicel and filter paper, indicating that Cel16A is an endo-ß-1,3(4)-glucanases. Recombinant Cel16A had a pH optimum at 5.5 and a temperature optimum at 55 °C with a specific activity of 693 U/mg toward barley ß-glucan. It exhibited good stability over pH 5.0-9.0 and at temperatures up to 50 °C, retaining over 80% maximum activity. The K and V values of Cel16A for barley ß-glucan were 0.91 mg ml and 1530 µmol min ·mg , respectively. All these favorable enzymatic properties of Cel16A make it a good candidate for applications in various industries.
[Mh] Termos MeSH primário: Endo-1,3(4)-beta-Glucanase/metabolismo
Proteínas Fúngicas/metabolismo
Pichia/genética
Proteínas Recombinantes/metabolismo
Sordariales/química
beta-Glucanas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico
Cromatografia de Afinidade
Clonagem Molecular
Endo-1,3(4)-beta-Glucanase/genética
Endo-1,3(4)-beta-Glucanase/isolamento & purificação
Ensaios Enzimáticos
Estabilidade Enzimática
Proteínas Fúngicas/genética
Proteínas Fúngicas/isolamento & purificação
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Glucanos/metabolismo
Temperatura Alta
Concentração de Íons de Hidrogênio
Cinética
Peso Molecular
Pichia/metabolismo
Sinais Direcionadores de Proteínas/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Alinhamento de Sequência
Sordariales/enzimologia
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Glucans); 0 (Protein Sorting Signals); 0 (Recombinant Proteins); 0 (beta-Glucans); 9008-22-4 (laminaran); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase); M7F3LRN53I (lichenin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151128
[St] Status:MEDLINE


  6 / 99 MEDLINE  
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[PMID]:27810709
[Au] Autor:Mangan D; Liadova A; Ivory R; McCleary BV
[Ad] Endereço:Megazyme International Ireland, Bray Business Park, Southern Cross Road, Bray, County Wicklow, Ireland. Electronic address: david@megazyme.com.
[Ti] Título:Novel approaches to the automated assay of ß-glucanase and lichenase activity.
[So] Source:Carbohydr Res;435:162-172, 2016 Nov 29.
[Is] ISSN:1873-426X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:We report herein the development of a novel assay procedure for the measurement of ß-glucanase and lichenase (EC 3.2.1.73) in crude enzyme extracts. Two assay formats based on a) a direct cleavage or b) an enzyme coupled substrate were initially investigated. The 'direct cleavage' substrate, namely 4,6-O-benzylidene-2-chloro-4-nitrophenyl-ß-3 -cellotriosyl-ß-glucopyranoside (MBG4), was found to be the more generally applicable reagent. This substrate was fully characterised using a crude malt ß-glucanase extract, a bacterial lichenase (Bacillus sp.) and a non-specific endo-1,3(4)-ß-glucanase from Clostridium thermocellum (EC 3.2.1.6). Standard curves were derived that allow the assay absorbance response to be directly converted to ß-glucanase/lichenase activity on barley ß-glucan. The specificity of MBG4 was confirmed by analysing the action of competing glycosyl hydrolases that are typically found in malt on the substrate. Manual and automated assay formats were developed for the analysis of a) ß-glucanase in malt flour and b) lichenase enzyme extracts and the repeatability of these assays was fully investigated.
[Mh] Termos MeSH primário: Endo-1,3(4)-beta-Glucanase/metabolismo
Glicosídeo Hidrolases/metabolismo
beta-Glucanas/análise
[Mh] Termos MeSH secundário: Automação Laboratorial
Bacillus subtilis/enzimologia
Proteínas de Bactérias/metabolismo
Clostridium thermocellum/enzimologia
Hordeum/enzimologia
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (beta-Glucans); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase); EC 3.2.1.73 (licheninase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170227
[Lr] Data última revisão:
170227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE


  7 / 99 MEDLINE  
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[PMID]:26888054
[Au] Autor:Sakdapetsiri C; Fukuta Y; Aramsirirujiwet Y; Shirasaka N; Kitpreechavanich V
[Ad] Endereço:Faculty of Science, Department of Microbiology, Kasetsart University, Lat Yao, Chatuchak, Bangkok, Thailand.
[Ti] Título:Antagonistic activity of endo-ß-1,3-glucanase from a novel isolate, Streptomyces sp. 9X166, against black rot in orchids.
[So] Source:J Basic Microbiol;56(5):469-79, 2016 May.
[Is] ISSN:1521-4028
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A total of 123 actinomycetes was isolated from 12 varieties of wild orchids and screened for potential antagonistic activity against Phytophthora, which causes black rot disease in orchids. In vitro and in vivo experimental results revealed that Streptomyces sp. strain 9X166 showed the highest antagonistic activity; its ß-1,3-glucanase production ability was a key mechanism for growth inhibition of the pathogen. PCR amplification and DNA sequencing of the 16S ribosomal RNA gene allowed the identification of this strain, with high similarity (99.93%) to the novel species Streptomyces similaensis. The glucanase enzyme, purified to homogeneity by anion exchange and gel filtration chromatography, showed a specific activity of 58 U mg(-1) (a 3.9-fold increase) and yield of 6.4%. The molecular weight, as determined by SDS-PAGE and gel filtration, was approximately 99 and 80 kDa, respectively, suggesting that the enzyme was a monomer. The purified enzyme showed the highest substrate specificity to laminarin, indicating that it was ß-1,3-glucanase. The hydrolyzed products of cello-oligosaccharides suggested that this enzyme was endo-type ß-1,3-glucanase. Streptomyces sp. 9X166 culture filtrate, possessing ß-1,3-glucanase activity, could degrade both freeze-dried and living mycelium. This is the first report on a ß-1,3-glucanase-producing Streptomyces sp. that could be an effective biocontrol agent for black rot disease in orchids.
[Mh] Termos MeSH primário: Agentes de Controle Biológico/metabolismo
Endo-1,3(4)-beta-Glucanase/genética
Endo-1,3(4)-beta-Glucanase/metabolismo
Glucanos/metabolismo
Orchidaceae/parasitologia
Phytophthora/crescimento & desenvolvimento
Doenças das Plantas/parasitologia
Streptomyces/enzimologia
[Mh] Termos MeSH secundário: Eletroforese em Gel de Poliacrilamida
Oligossacarídeos/metabolismo
RNA Ribossômico 16S/genética
Streptomyces/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biological Control Agents); 0 (Glucans); 0 (Oligosaccharides); 0 (RNA, Ribosomal, 16S); 9008-22-4 (laminaran); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170217
[Lr] Data última revisão:
170217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160219
[St] Status:MEDLINE
[do] DOI:10.1002/jobm.201500709


  8 / 99 MEDLINE  
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[PMID]:26837217
[Au] Autor:Meng DD; Wang B; Ma XQ; Ji SQ; Lu M; Li FL
[Ad] Endereço:Key Laboratory of Biofuels, Shandong Provincial Key Laboratory of Energy Genetics, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.
[Ti] Título:Characterization of a thermostable endo-1,3(4)-ß-glucanase from Caldicellulosiruptor sp. strain F32 and its application for yeast lysis.
[So] Source:Appl Microbiol Biotechnol;100(11):4923-34, 2016 Jun.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:ß-1,3-Glucans, important structural components of cell wall or nutritional components of the endosperm, are extensively found in bacteria, fungi, yeast, algae, and plants. The structural complexity of ß-1,3-glucans implies that the enzymatic depolymerization of polysaccharides needs combined activities of distinct enzymes. In this study, Lam16A-GH, the catalytic module of a putative glycoside hydrolase (GH) family 16 laminarinase/lichenase from thermophilic bacterium Caldicellulosiruptor sp. F32, was purified and characterized through heterologous expression in Escherichia coli. Lam16A-GH can hydrolyze both ß-1,3-glucan (laminarin) and ß-1,3-1,4-glucan (barley ß-glucan) revealed by analysis of the products of polysaccharide degradation using thin-layer chromatography (TLC). The time required for the loss of 50 % of its activity is 45 h under the optimal condition of 75 °C and pH 6.5. Oligosaccharides degradation assay indicated that Lam16A-GH can catalyze endo-hydrolysis of the ß-1,4 glycosidic linkage adjacent to a 3-O-substituted glucosyl residue in the mixed linked ß-glucans, as well as the ß-1,3 linkage. The survival rate of Saccharomyces cerevisiae cells depends on the addition of Lam16A-GH, and the cytoplasm protein was released from the apparently deconstructed yeast cells. These results indicate that the bi-functional thermostable Lam16A-GH exhibits unique enzymatic properties and potential for yeast lysis.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Endo-1,3(4)-beta-Glucanase/metabolismo
Saccharomyces cerevisiae/citologia
Thermoanaerobacterium/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Parede Celular/química
Cromatografia em Camada Delgada
Clonagem Molecular
Endo-1,3(4)-beta-Glucanase/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Glucanos/química
Glicosídeo Hidrolases/genética
Glicosídeo Hidrolases/metabolismo
Concentração de Íons de Hidrogênio
Hidrólise
Oligossacarídeos/química
Especificidade por Substrato
Temperatura Ambiente
Thermoanaerobacterium/genética
Regulação para Cima
beta-Glucanas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Glucans); 0 (Oligosaccharides); 0 (beta-Glucans); 9051-96-1 (1,4-glucan); 9051-97-2 (beta-1,3-glucan); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase); EC 3.2.1.73 (licheninase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170207
[Lr] Data última revisão:
170207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160204
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7334-x


  9 / 99 MEDLINE  
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[PMID]:26745986
[Au] Autor:Xu T; Zhu T; Li S
[Ad] Endereço:College of Forestry, Sichuan Agricultural University, Ya'an, 625014, China. sweetinxt@163.com.
[Ti] Título:ß-1,3-1,4-glucanase gene from Bacillus velezensis ZJ20 exerts antifungal effect on plant pathogenic fungi.
[So] Source:World J Microbiol Biotechnol;32(2):26, 2016 Feb.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Bacillus velezensis is a known antifungal bacteria. To understand the role of ß-1, 3-1, 4-glucanase played on B. velezensis about the mechanism which exerts effect on fungi, we isolated and cloned the ß-1, 3-1, 4-glucanase gene (Bglu1) from B. velezensis ZJ20. The Bglu1 open reading frame was 732 bp that encoded a protein with 243 amino acids and a calculated molecular weight of 27.3 kDa. The same gene without the signal peptide, termed Bglu2, was also cloned and expressed in E. coli BL21. Among the two variants, only Bglu2 protein was expressed. Purified Bglu2 could be eluted with imidazole solution at concentrations ranging from 100 to 500 mM although the highest expression was observed at 150 and 200 mM and the purest was at 500 mM. In addition, activity of the crude enzyme was 1527 U ml(-1) and the highest activity of the purified enzyme was 1706 U ml(-1). The purified ß-1, 3-1, 4-glucanase had activity on a wide range of pH and temperatures and displayed optimal activity at pH 5.0 and 35 °C. More importantly, the mycelial morphology of three pathogenic fungi was destroyed by the purified ß-1, 3-1, 4-glucanase. In conclusion, ß-1, 3-1, 4-glucanase from B. velezensis ZJ20 can be highly expressed in E. coli BL21 and the recombinant protein is pathogenic to fungi.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Bacillus/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/farmacologia
Endo-1,3(4)-beta-Glucanase/genética
Endo-1,3(4)-beta-Glucanase/farmacologia
Fungos/efeitos dos fármacos
Doenças das Plantas/microbiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antifúngicos/metabolismo
Bacillus/enzimologia
Proteínas de Bactérias/biossíntese
Proteínas de Bactérias/isolamento & purificação
Sequência de Bases
Clonagem Molecular
Endo-1,3(4)-beta-Glucanase/biossíntese
Endo-1,3(4)-beta-Glucanase/isolamento & purificação
Escherichia coli/enzimologia
Escherichia coli/genética
Fungos/citologia
Fungos/patogenicidade
Expressão Gênica
Fases de Leitura Aberta
Controle Biológico de Vetores/métodos
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Bacterial Proteins); 0 (Recombinant Proteins); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160110
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-015-1985-0


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[PMID]:26507654
[Au] Autor:McGregor N; Morar M; Fenger TH; Stogios P; Lenfant N; Yin V; Xu X; Evdokimova E; Cui H; Henrissat B; Savchenko A; Brumer H
[Ad] Endereço:From the Michael Smith Laboratories and Department of Chemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada.
[Ti] Título:Structure-Function Analysis of a Mixed-linkage ß-Glucanase/Xyloglucanase from the Key Ruminal Bacteroidetes Prevotella bryantii B(1)4.
[So] Source:J Biol Chem;291(3):1175-97, 2016 Jan 15.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The recent classification of glycoside hydrolase family 5 (GH5) members into subfamilies enhances the prediction of substrate specificity by phylogenetic analysis. However, the small number of well characterized members is a current limitation to understanding the molecular basis of the diverse specificity observed across individual GH5 subfamilies. GH5 subfamily 4 (GH5_4) is one of the largest, with known activities comprising (carboxymethyl)cellulases, mixed-linkage endo-glucanases, and endo-xyloglucanases. Through detailed structure-function analysis, we have revisited the characterization of a classic GH5_4 carboxymethylcellulase, PbGH5A (also known as Orf4, carboxymethylcellulase, and Cel5A), from the symbiotic rumen Bacteroidetes Prevotella bryantii B14. We demonstrate that carboxymethylcellulose and phosphoric acid-swollen cellulose are in fact relatively poor substrates for PbGH5A, which instead exhibits clear primary specificity for the plant storage and cell wall polysaccharide, mixed-linkage ß-glucan. Significant activity toward the plant cell wall polysaccharide xyloglucan was also observed. Determination of PbGH5A crystal structures in the apo-form and in complex with (xylo)glucan oligosaccharides and an active-site affinity label, together with detailed kinetic analysis using a variety of well defined oligosaccharide substrates, revealed the structural determinants of polysaccharide substrate specificity. In particular, this analysis highlighted the PbGH5A active-site motifs that engender predominant mixed-linkage endo-glucanase activity vis à vis predominant endo-xyloglucanases in GH5_4. However the detailed phylogenetic analysis of GH5_4 members did not delineate particular clades of enzymes sharing these sequence motifs; the phylogeny was instead dominated by bacterial taxonomy. Nonetheless, our results provide key enzyme functional and structural reference data for future bioinformatics analyses of (meta)genomes to elucidate the biology of complex gut ecosystems.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Celulase/metabolismo
Endo-1,3(4)-beta-Glucanase/metabolismo
Glicosídeo Hidrolases/metabolismo
Modelos Moleculares
Prevotella/enzimologia
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Apoenzimas/antagonistas & inibidores
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise
Domínio Catalítico
Celulase/antagonistas & inibidores
Celulase/química
Celulase/genética
Celulose/química
Celulose/metabolismo
Endo-1,3(4)-beta-Glucanase/antagonistas & inibidores
Endo-1,3(4)-beta-Glucanase/química
Endo-1,3(4)-beta-Glucanase/genética
Inibidores Enzimáticos/química
Inibidores Enzimáticos/metabolismo
Inibidores Enzimáticos/farmacologia
Glucanos/química
Glucanos/metabolismo
Glicosídeo Hidrolases/antagonistas & inibidores
Glicosídeo Hidrolases/química
Glicosídeo Hidrolases/genética
Temperatura Alta
Concentração de Íons de Hidrogênio
Mutação
Filogenia
Conformação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Xilanos/química
Xilanos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Bacterial Proteins); 0 (Enzyme Inhibitors); 0 (Glucans); 0 (Recombinant Proteins); 0 (Xylans); 37294-28-3 (xyloglucan); 9004-34-6 (Cellulose); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.- (endoglucanase Cel5A); EC 3.2.1.- (xyloglucan endo(1-4)-beta-D-glucanase); EC 3.2.1.4 (Cellulase); EC 3.2.1.6 (Endo-1,3(4)-beta-Glucanase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170118
[Lr] Data última revisão:
170118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151029
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.691659



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