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Id: biblio-886801
Autor: MARCO, ÉVILIN G DE; HECK, KARINA; MARTOS, EMERSON T; VAN DER SAND, SUELI T.
Título: Purification and characterization of a thermostable alkaline cellulase produced by Bacillus licheniformis 380 isolated from compost
Fonte: An. acad. bras. ciênc;89(3,supl):2359-2370, 2017. tab, graf.
Idioma: en.
Resumo: ABSTRACT During composting processes, the degradation of organic waste is accomplished and driven by a succession of microbial populations exhibiting a broad range of functional competencies. A total of 183 bacteria, isolated from a composting process, were evaluated for cellulase activity at different temperatures (37, 50, 60, and 70°C) and pH values. Out of the 22 isolates that showed activity, isolate 380 showed the highest cellulase activity. Its ability to produce cellulase was evaluated in culture medium supplemented with carboxymethyl cellulose, microcrystalline cellulose, wheat straw, and rice husk. The culture medium supplemented with carboxymethyl cellulose induced higher enzyme activity after 6 hours of incubation (0.12 UEA mL-1 min-1). For wheat straw and rice husk, the results were 0.08 UEA mL-1 min-1 for both, while for microcrystalline cellulose, 0.04 UEA mL-1 min-1 were observed. The highest carboxymethyl cellulase activity was observed at 60°C (0.14 UEA mL-1 min-1) for both crude and partially purified enzyme after 30 and 120 min of incubation, respectively. Alkalinization of the medium was observed during cultivation in all substrates. The cellulase had a molecular mass of 20 kDa determined by SDS-Page. Isolate 380 was identified as Bacillus licheniformis. This work provides a basis for further studies on composting optimization.
Descritores: Carboximetilcelulose Sódica/farmacologia
Celulase/isolamento & purificação
Celulase/biossíntese
Meios de Cultura/farmacologia
Bacillus licheniformis/enzimologia
-Especificidade por Substrato
Eletroforese em Gel de Poliacrilamida
Bacillus licheniformis/efeitos dos fármacos
Temperatura Alta
Responsável: BR1.1 - BIREME


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Id: biblio-951810
Autor: Rungrattanakasin, Budsayachat; Premjet, Siripong; Thanonkeo, Sudarat; Klanrit, Preekamol; Thanonkeo, Pornthap.
Título: Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
Fonte: Braz. j. microbiol;49(3):647-655, July-Sept. 2018. graf.
Idioma: en.
Resumo: Abstract An intronless endoglucanase from thermotolerant Aspergillus fumigatus DBINU-1 was cloned, characterized and expressed in the yeast Kluyveromyces lactis. The full-length open reading frame of the endoglucanase gene from A. fumigatus DBiNU-1, designated Cel7, was 1383 nucleotides in length and encoded a protein of 460 amino acid residues. The predicted molecular weight and the isoelectric point of the A. fumigatus Cel7 gene product were 48.19 kDa and 5.03, respectively. A catalytic domain in the N-terminal region and a fungal type cellulose-binding domain/module in the C-terminal region were detected in the predicted polypeptide sequences. Furthermore, a signal peptide with 20 amino acid residues at the N-terminus was also detected in the deduced amino acid sequences of the endoglucanase from A. fumigatus DBiNU-1. The endoglucanase from A. fumigatus DBiNU-1 was successfully expressed in K. lactis, and the purified recombinant enzyme exhibited its maximum activity at pH 5.0 and 60 °C. The enzyme was very stable in a pH range from 4.0 to 8.0 and a temperature range from 30 to 60 °C. These features make it suitable for application in the paper, biofuel, and other chemical production industries that use cellulosic materials.
Descritores: Aspergillus fumigatus/enzimologia
Proteínas Fúngicas/genética
Proteínas Fúngicas/química
Expressão Gênica
Celulase/genética
Celulase/química
Clonagem Molecular
-Aspergillus fumigatus/genética
Especificidade por Substrato
Estabilidade Enzimática
Kluyveromyces/genética
Kluyveromyces/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/química
Proteínas Fúngicas/metabolismo
Celulase/metabolismo
Temperatura Alta
Concentração de Íons de Hidrogênio
Responsável: BR1.1 - BIREME


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Id: lil-780841
Autor: Bottino, Flávia; Cunha-Santino, Marcela Bianchessi; Bianchini Jr, Irineu.
Título: Cellulase activity and dissolved organic carbon release from lignocellulose macrophyte-derived in four trophic conditions
Fonte: Braz. j. microbiol;47(2):352-358, Apr.-June 2016. tab, graf.
Idioma: en.
Projeto: São Paulo Research Foundation.
Resumo: Abstract Considering the importance of lignocellulose macrophyte-derived for the energy flux in aquatic ecosystems and the nutrient concentrations as a function of force which influences the decomposition process, this study aims to relate the enzymatic activity and lignocellulose hydrolysis in different trophic statuses. Water samples and two macrophyte species were collected from the littoral zone of a subtropical Brazilian Reservoir. A lignocellulosic matrix was obtained using aqueous extraction of dried plant material (≈40 °C). Incubations for decomposition of the lignocellulosic matrix were prepared using lignocelluloses, inoculums and filtered water simulating different trophic statuses with the same N:P ratio. The particulate organic carbon and dissolved organic carbon (POC and DOC, respectively) were quantified, the cellulase enzymatic activity was measured by releasing reducing sugars and immobilized carbon was analyzed by filtration. During the cellulose degradation indicated by the cellulase activity, the dissolved organic carbon daily rate and enzyme activity increased. It was related to a fast hydrolysable fraction of cellulose that contributed to short-term carbon immobilization (ca. 10 days). After approximately 20 days, the dissolved organic carbon and enzyme activity were inversely correlated suggesting that the respiration of microorganisms was responsible for carbon mineralization. Cellulose was an important resource in low nutrient conditions (oligotrophic). However, the detritus quality played a major role in the lignocelluloses degradation (i.e., enzyme activity) and carbon release.
Descritores: Bactérias/enzimologia
Proteínas de Bactérias/metabolismo
Celulase/metabolismo
Araceae/metabolismo
Paspalum/metabolismo
Água Doce/química
Lignina/metabolismo
-Brasil
Carbono/metabolismo
Celulose/genética
Celulose/metabolismo
Ecossistema
Araceae/crescimento & desenvolvimento
Araceae/microbiologia
Paspalum/crescimento & desenvolvimento
Paspalum/microbiologia
Água Doce/microbiologia
Responsável: BR1.1 - BIREME


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Id: biblio-1048705
Autor: Felber, Aretusa Cristina; Specian, Vânia; Orlandelli, Ravely Casarotti; Costa, Alessandra Tenório; Polonio, Julio Cesar; Mourão, Káthia Socorro Mathias; Pamphile, João Alencar.
Título: Endoglucanase production by endophytic fungi isolated from vitis labrusca l. with peanut hull and sawdust as substrates / Produção de endoglucanase por fungos endofíticos isolados de Vitis labrusca L. utilizando casca de amendoim e serragem como substratos
Fonte: Biosci. j. (Online);35(3):933-940, may./jun. 2019. tab.
Idioma: en.
Resumo: Endoglucanases are enzymes widely employed in different industrial fields, albeit with high production costs. Studies on new microbial sources and low-cost substrates are highly relevant, including those on agro-industrial. Current analysis evaluates peanut hull (PH) and sawdust (SD) as substrates for submerged cultures of 14 endophytic fungi isolated from grapevine (Vitis labrusca L.) cultivars Bordô and Concord. Endophytes were grown on a carboxymethylcellulose (CMC) medium and the cup plate assay showed that eight strains (belonging to genera Cochliobolus, Diaporthe, Fusarium and Phoma) had positive results: enzymatic halos ranged from 10.8±0.02to 15.5±0.07 mm in diameter. Diaporthe sp. strains (GenBank accession codes KM362392, KM362368 and KM362378) and Fusariumculmorum KM362384 were highlighted as the most promising sources. Further, PH and SD as substrates for the fermentation of these fungi were evaluated by the cup plate assay and endoglucanase activity assay. Highest halo diameters were obtained for Diaporthe sp. KM362392: 16.1±0.01 mm (CMC), 14.5±0.01 mm (PH) and 14.7±0.03 mm (SD). The fungus also presented the highest levels of endoglucanase activity: analysis of variance revealed that CMC (3.52±0.98 µmol/min), PH (2.93±0.23 µmol/min) and SD (3.26±0.38 µmol/min) were similarly efficient as substrates. Results deepen knowledge on V. labrusca endophytes that may be endoglucanase sources, eventhough further optimizations in submerged cultures with PH and SD should be undertaken to increase theenzymatic production from these wastes.

Endoglucanases são enzimas amplamente empregadas em diferentes setores industriais; embora sua produção apresente custos elevados. Estudos sobre novas fontes microbianas e substratos mais baratos são de grande importância, incluindo os resíduos agroindustriais. Nesse estudo, casca de amendoim (CA) e serragem (SE) foram testadas como substratos para o cultivo submerso de 14 fungos endofíticos isolados das cultivares Bordô e Concord de videira (Vitis labrusca L.) Os endófitos foram crescidos em meio contendo carboximetilcelulose (CMC) e o ensaio cup plate mostrou resultados positivos para oito fungos (pertencentes aos gêneros Cochliobolus, Diaporthe, Fusarium and Phoma); os halos enzimáticos variaram entre 10,8±0,02 e 15,5±0,07 mm de diâmetro. Linhagens de Diaporthe sp. (códigos de acesso no GenBank KM362392, KM362368 e KM362378) e Fusariumculmorum KM362384 se destacaram como produtores mais promissores. Então, o uso de CA e SE como substratos para a fermentação desses fungos foi avaliado pelo ensaio cup plate e pela quantificação da atividade de endoglucanase. Os maiores halos enzimáticos foram obtidos para Diaporthe sp. KM362392: 16,1±0,01 mm (CMC), 14,5±0,01 mm (CA) e 14,7±0,03 mm (SE). Esse fungo também apresentou os maiores níveis de endoglucanase: a análise de variância revelou que CMC (3,52±0,98 µmol/min), CA (2,93±0,23 µmol/min) e SE (3,26±0,38 µmol/min) foram substratos similarmente eficientes. Esses resultados expandem o conhecimento sobre endófitos de V. labrusca que são fontes de endoglucanases; futuras otimizações quanto ao cultivo submerso com CA e SE podem ser utilizadas para aumentar a produção enzimática a partir do uso desses resíduos.
Descritores: Resíduos
Celulase
Substratos
Enzimas
Agroindústria
Endófitos
Responsável: BR396.1 - Biblioteca Central


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ASTOLFI-FILHO, SPARTACO
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Id: biblio-1022139
Autor: Santa-Rosa, Pamella S; Souza, Anita L; Roque, Rosemary A; Andrade, Edmar V; Astolfi-Filho, Spartaco; Mota, Adolfo J; Nunes-Silva, Carlos G.
Título: Production of thermostable ß-glucosidase and CMCase by Penicillium sp: LMI01 isolated from the Amazon region
Fonte: Electron. j. biotechnol;31:84-92, Jan. 2018. graf, tab, ilus.
Idioma: en.
Projeto: Fundação de Amparo a Pesquisa do Amazonas, FAPEAM - PAPPE Integração; . Coordenação de Aperfeiçoamento de Pessoal Nível Superior, CAPES; . Conselho Nacional de Desenvolvimento Científico e Tecnológico, CNPq.
Resumo: Background: Cellulolytic enzymes of microbial origin have great industrial importance because of their wide application in various industrial sectors. Fungi are considered the most efficient producers of these enzymes. Bioprospecting survey to identify fungal sources of biomass-hydrolyzing enzymes from a high-diversity environment is an important approach to discover interesting strains for bioprocess uses. In this study, we evaluated the production of endoglucanase (CMCase) and ß-glucosidase, enzymes from the lignocellulolytic complex, produced by a native fungus. Penicillium sp. LMI01 was isolated from decaying plant material in the Amazon region, and its performance was compared with that of the standard isolate Trichoderma reesei QM9414 under submerged fermentation conditions. Results: The effectiveness of LMI01 was similar to that of QM9414 in volumetric enzyme activity (U/mL); however, the specific enzyme activity (U/mg) of the former was higher, corresponding to 24.170 U/mg of CMCase and 1.345 U/mg of ß-glucosidase. The enzymes produced by LMI01 had the following physicochemical properties: CMCase activity was optimal at pH 4.2 and the ß-glucosidase activity was optimal at pH 6.0. Both CMCase and ß-glucosidase had an optimum temperature at 60°C and were thermostable between 50 and 60°C. The electrophoretic profile of the proteins secreted by LMI01 indicated that this isolate produced at least two enzymes with CMCase activity, with approximate molecular masses of 50 and 35 kDa, and ß-glucosidases with molecular masses between 70 and 100 kDa. Conclusions: The effectiveness and characteristics of these enzymes indicate that LMI01 can be an alternative for the hydrolysis of lignocellulosic materials and should be tested in commercial formulations.
Descritores: Penicillium/enzimologia
Celulase/biossíntese
beta-Glucosidase/biossíntese
-Oligossacarídeos
Temperatura
Trichoderma/enzimologia
Estabilidade Enzimática
Celulase/metabolismo
beta-Glucosidase/metabolismo
Ecossistema Amazônico
Biocatálise
Fermentação
Concentração de Íons de Hidrogênio
Hidrólise
Lignina/metabolismo
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1010399
Autor: Seneesrisakul, Kessara; Albayrak Guralp, Saadet; Gulari, Erdogan; Chavadej, Sumaeth.
Título: Escherichia coli expressing endoglucanase gene from Thai higher termite bacteria for enzymatic and microbial hydrolysis of cellulosic materials
Fonte: Electron. j. biotechnol;27:70-79, May. 2017. tab, ilus, graf.
Idioma: en.
Resumo: Background: Endoglucanase plays a major role in initiating cellulose hydrolysis. Various wild-type strains were searched to produce this enzyme, but mostly low extracellular enzyme activities were obtained. To improve extracellular enzyme production for potential industrial applications, the endoglucanase gene of Bacillus subtilis M015, isolated from Thai higher termite, was expressed in a periplasmic-leaky Escherichia coli. Then, the crude recombinant endoglucanase (EglS) along with a commercial cellulase (Cel) was used for hydrolyzing celluloses and microbial hydrolysis using whole bacterial cells. Results: E. coli Glu5 expressing endoglucanase at high levels was successfully constructed. It produced EglS (55 kDa) with extracellular activity of 18.56 U/mg total protein at optimal hydrolytic conditions (pH 4.8 and 50°C). EglS was highly stable (over 80% activity retained) at 40­50°C after 100 h. The addition of EglS significantly improved the initial sugar production rates of Cel on the hydrolysis of carboxymethyl cellulose (CMC), microcrystalline cellulose, and corncob about 5.2-, 1.7-, and 4.0-folds, respectively, compared to those with Cel alone. E. coli Glu5 could secrete EglS with high activity in the presence of glucose (1% w/v) and Tween 80 (5% w/v) with low glucose consumption. Microbial hydrolysis of CMC using E. coli Glu5 yielded 26 mg reducing sugar/g CMC at pH 7.0 and 37°C after 48 h. Conclusions: The recombinant endoglucanase activity improved by 17 times compared with that of the native strain and could greatly enhance the enzymatic hydrolysis of all studied celluloses when combined with a commercial cellulase.
Descritores: Bacillus subtilis/enzimologia
Celulase/metabolismo
Isópteros/microbiologia
-Tailândia
Proteínas Recombinantes/metabolismo
Celulase/genética
Celulose
Amplificação de Genes
Agricultura
Escherichia coli/metabolismo
Hidrólise
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-966995
Autor: Zamani, Hojjatolah; Salehzadeh, Ali; Abdolhosseini, Mansoreh.
Título: Isolation and molecular identification of a cellulotic bacterium from muncipal waste and investigation of its cellulase production / Isolamento e identificação molecular de uma bactéria celulolítica do lixo municipal e investigação de sua produção de celulase
Fonte: Biosci. j. (Online);34(3):761-768, mai/jun. 2018. graf, tab.
Idioma: en.
Resumo: Municipal waste is rich in lignocellulosic compounds which contain cellulose, lignin and hemicellulose. Microorganisms can break down such compounds and convert them into glucose and other carbohydrates. The current study was performed to isolate and identify cellulolytic bacteria in municipal waste. Municipal waste samples were collected and plated on Carboxymethyl cellulose (CMC) agar. Preliminary identification of the isolates was performed using standard biochemical assays. The activity of carboxymethyl cellulose (CMCase) was specified through measuring the release of reducing sugars from CMC. Different nitrogen sources at various concentrations and initial pH values were evaluated for their effect on enzyme production. Further the enzyme production was determined at different fermentation times. Molecular identification was then performed using bacterial 16s rRNA gene amplification and sequencing. A cellulolytic bacterium was isolated from municipal waste samples and identified based on morphological, physiological and biochemical characteristics along with 16S rRNA analysis. The isolated bacterium was identified as Bacillus subtilis (accession number: KU681044). Whose growth characteristics showed that its growth curve entered the logarithmic phase following 10­18 h with the stable growth phase ranging from 23 to 37 h. The optimal carbon source for fermentation was 1% rice hull, with the nitrogen source comprised of 2% peptone and yeast extract. The the minimum CMCase activity was observed at an initial medium pH of 4.0, while the maximum was observed at pH 7. The strain grew vigorously and the cellulase yield was high at 6­24 h fermentation time period. The isolated bacteria showed the degrading potential of cellulose which could be employed in local industrial process.

Resíduos urbanos são ricos em compostos lignocelulósicos que contêm celulose, lignina e hemicelulose. Microrganismos podem quebrar esses compostos e convertê-los em glicose e outros carboidratos. O presente estudo foi realizado para isolar e identificar bactérias celulolíticas em resíduos urbanos. Amostras de resíduos municipais foram coletadas e plaqueadas em ágar Carboximetilcelulose (CMC). A identificação preliminar dos isolados foi realizada utilizando ensaios bioquímicos padrão. A atividade da carboximetilcelulose (CMCase) foi especificada através da medição da liberação de açúcares redutores da CMC. Diferentes fontes de nitrogênio em várias concentrações e valores iniciais de pH foram avaliados quanto ao seu efeito na produção de enzimas. Além disso, a produção de enzima foi determinada em diferentes tempos de fermentação. A identificação molecular foi então realizada utilizando amplificação e sequenciamento do gene bacteriano 16s rRNA. Uma bactéria celulolítica foi isolada de amostras de resíduos urbanos e identificada com base em características morfológicas, fisiológicas e bioquímicas, juntamente com a análise 16S rRNA. A bactéria isolada foi identificada como Bacillus subtilis (número de acesso: KU681044). Cujas características de crescimento mostraram que sua curva de crescimento entrou na fase logarítmica após 10-18 h com a fase de crescimento estável variando de 23 a 37 h. A fonte de carbono ótima para a fermentação foi 1% de casca de arroz, com a fonte de nitrogênio composta de 2% de peptona e extrato de levedura. A atividade mínima de CMCase foi observada em um pH médio inicial de 4,0, enquanto a máxima foi observada em pH 7. A linhagem cresceu vigorosamente e o rendimento de celulase foi alto no período de 6 a 24 horas de fermentação. As bactérias isoladas mostraram o potencial de degradação da celulose que poderia ser empregada no processo industrial local.
Descritores: Bacillus subtilis
Resíduos
Carboximetilcelulose Sódica
Celulase
-Bioquímica
Resíduos Sólidos
Responsável: BR396.1 - Biblioteca Central


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Id: biblio-889226
Autor: Thomas, Lebin; Ram, Hari; Singh, Ved Pal.
Título: Inducible cellulase production from an organic solvent tolerant Bacillus sp. SV1 and evolutionary divergence of endoglucanase in different species of the genus Bacillus
Fonte: Braz. j. microbiol;49(2):429-442, Apr.-June 2018. tab, graf.
Idioma: en.
Resumo: Abstract Bacteria are important sources of cellulases with various industrial and biotechnological applications. In view of this, a non-hemolytic bacterial strain, tolerant to various environmental pollutants (heavy metals and organic solvents), showing high cellulolytic index (7.89) was isolated from cattle shed soil and identified as Bacillus sp. SV1 (99.27% pairwise similarity with Bacillus korlensis). Extracellular cellulases showed the presence of endoglucanase, total cellulase and β-glucosidase activities. Cellulase production was induced in presence of cellulose (3.3 times CMCase, 2.9 times FPase and 2.1 times β-glucosidase), and enhanced (115.1% CMCase) by low-cost corn steep solids. An in silico investigation of endoglucanase (EC 3.2.1.4) protein sequences of three Bacillus spp. as query, revealed their similarities with members of nine bacterial phyla and to Eukaryota (represented by Arthropoda and Nematoda), and also highlighted of a convergent and divergent evolution from other enzymes of different substrate [(1,3)-linked beta-d-glucans, xylan and chitosan] specificities. Characteristic conserved signature indels were observed among members of Actinobacteria (7 aa insert) and Firmicutes (9 aa insert) that served as a potential tool in support of their relatedness in phylogenetic trees.
Descritores: Bacillus/enzimologia
Celulase/genética
Celulase/metabolismo
Evolução Molecular
-Bacillus/crescimento & desenvolvimento
Bacillus/isolamento & purificação
Celulose/metabolismo
Biologia Computacional
Fezes/microbiologia
Regulação Bacteriana da Expressão Gênica
Regulação Enzimológica da Expressão Gênica
Mutação INDEL
Análise de Sequência de DNA
Homologia de Sequência
Especificidade por Substrato
Zea mays/metabolismo
Limites: Animais
Bovinos
Responsável: BR1.1 - BIREME


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Id: biblio-889172
Autor: Song, Yun-Hee; Lee, Kyung-Tai; Baek, Jin-Young; Kim, Min-Ju; Kwon, Mi-Ra; Kim, Young-Joo; Park, Mi-Rim; Ko, Haesu; Lee, Jin-Sung; Kim, Keun-Sung.
Título: Isolation and characterization of a novel endo-beta-1, 4-glucanase from a metagenomic library of the black-goat rumen
Fonte: Braz. j. microbiol;48(4):801-808, Oct.-Dec. 2017. tab, graf.
Idioma: en.
Resumo: ABSTRACT The various types of lignocellulosic biomass found in plants comprise the most abundant renewable bioresources on Earth. In this study, the ruminal microbial ecosystem of black goats was explored because of their strong ability to digest lignocellulosic forage. A metagenomic fosmid library containing 115,200 clones was prepared from the black-goat rumen and screened for a novel cellulolytic enzyme. The KG35 gene, containing a novel glycosyl hydrolase family 5 cellulase domain, was isolated and functionally characterized. The novel glycosyl hydrolase family 5 cellulase gene is composed of a 963-bp open reading frame encoding a protein of 320 amino acid residues (35.1 kDa). The deduced amino acid sequence showed the highest sequence identity (58%) for sequences from the glycosyl hydrolase family 5 cellulases. The novel glycosyl hydrolase family 5 cellulase gene was overexpressed in Escherichia coli. Substrate specificity analysis revealed that this recombinant glycosyl hydrolase family 5 cellulase functions as an endo-β-1,4-glucanase. The recombinant KG35 endo-β-1,4-glucanase showed optimal activity within the range of 30-50 °C at a pH of 6-7. The thermostability was retained and the pH was stable in the range of 30-50 °C at a pH of 5-7.
Descritores: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Bactérias/enzimologia
Celulase/química
Celulase/genética
Rúmen/microbiologia
-Proteínas de Bactérias/metabolismo
Bactérias/classificação
Bactérias/genética
Bactérias/isolamento & purificação
Celulase/metabolismo
Clonagem Molecular
Estabilidade Enzimática
Microbioma Gastrointestinal
Cabras
Concentração de Íons de Hidrogênio
Metagenoma
Metagenômica
Limites: Animais
Responsável: BR1.1 - BIREME


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Id: lil-741270
Autor: Avellaneda-Torres, Lizeth Manuela; Pulido, Claudia Patricia Guevara; Rojas, Esperanza Torres.
Título: Assessment of cellulolytic microorganisms in soils of Nevados Park, Colombia
Fonte: Braz. j. microbiol;45(4):1211-1220, Oct.-Dec. 2014. graf, mapas, tab.
Idioma: en.
Projeto: Colciencias; . MAVDT; . UAESPNN.
Resumo: A systematized survey was conducted to find soil-borne microbes that degrade cellulose in soils from unique ecosystems, such as the Superpáramo, Páramo, and the High Andean Forest in the Nevados National Natural Park (NNNP), Colombia. These high mountain ecosystems represent extreme environments, such as high levels of solar radiation, low atmospheric pressure, and extreme daily changes in temperature. Cellulolytic activity of the microorganisms was evaluated using qualitative tests, such as growth in selective media followed by staining with congo red and iodine, and quantitative tests to determine the activity of endoglucanase, β-glucosidase, exoglucanase, and total cellulase. Microorganisms were identified using molecular markers, such as the 16S rRNA gene for bacteria and the internal transcribed spacer region (ITS) of ribosomal DNA for fungi. Multivariate statistical analysis (MVA) was used to select microorganisms with high cellulolytic capacity. A total of 108 microorganisms were isolated from the soils and, in general, the enzymatic activities of fungi were higher than those of bacteria. Our results also found that none of the organisms studied were able to degrade all the components of the cellulose and it is therefore suggested that a combination of bacteria and/or fungi with various enzymatic activities be used to obtain high total cellulolytic activity. This study gives an overview of the potential microorganism that could be used for cellulose degradation in various biotechnological applications and for sustainable agricultural waste treatment.
Descritores: Bactérias/isolamento & purificação
Bactérias/metabolismo
Celulose/metabolismo
Fungos/isolamento & purificação
Fungos/metabolismo
Microbiologia do Solo
-Bactérias/classificação
Bactérias/genética
Colômbia
Celulase/análise
DNA Bacteriano/química
DNA Bacteriano/genética
DNA Fúngico/química
DNA Fúngico/genética
DNA de Helmintos/química
DNA de Helmintos/genética
DNA Espaçador Ribossômico/química
DNA Espaçador Ribossômico/genética
DNA Ribossômico/química
DNA Ribossômico/genética
Fungos/classificação
Fungos/genética
Hidrólise
/genética
RNA, RIBOSOMAL, ABNORMALITIES, MULTIPLES/genética
Análise de Sequência de DNA
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde