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Id: biblio-886625
Autor: GOLUNSKI, SIMONE; SILVA, MARCELI F; MARQUES, CAMILA T; ROSSETO, VANUSA; KAIZER, ROSILENE R; MOSSI, ALTEMIR J; RIGO, DIANE; DALLAGO, ROGÉRIO M; DI LUCCIO, MARCO; TREICHEL, HELEN.
Título: Purification of inulinases by changing the ionic strength of the medium and precipitation with alcohols
Fonte: An. acad. bras. ciênc;89(1):57-63, Jan,-Mar. 2017. tab.
Idioma: en.
Resumo: ABSTRACT The present study evaluated the purification of inulinase by changing the ionic strength of the medium by addition of NaCl and CaCl2 followed by precipitation with n-propyl alcohol or iso-propyl alcohol. The effects of the concentration of alcohols and the rate of addition of alcohols in the crude extract on the purification yield and purification factor were evaluated. Precipitation caused an activation of enzyme and allowed purification factors up to 2.4-fold for both alcohols. The purification factor was affected positively by the modification of the ionic strength of the medium to 0.5 mol.L-1 NaCl before precipitation with the alcohol (n-propyl or iso-propyl). A purification factor of 4.8-fold and an enzyme yield of 78.1 % could be achieved by the addition of 0.5 mol.L-1 of NaCl to the crude extract, followed by the precipitation with 50 % (v/v) of n-propyl alcohol, added at a flow rate of 19.9 mL/min.
Descritores: Concentração Osmolar
Precipitação Química
Álcoois/química
Glicosídeo Hidrolases/isolamento & purificação
Glicosídeo Hidrolases/química
-Valores de Referência
Sais/química
Solventes/química
Kluyveromyces/isolamento & purificação
Kluyveromyces/química
Cloreto de Cálcio/química
Cloreto de Sódio/química
Reprodutibilidade dos Testes
Meios de Cultura/química
Tipo de Publ: Estudo de Avaliação
Responsável: BR1.1 - BIREME


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Id: biblio-1053491
Autor: Tian, Kangming; Wang, Jun; Zhang, Zhimeng; Cheng, Lei; Jin, Peng; Singh, Suren; Prior, Bernard A; Wang, Zheng-Xiang.
Título: Enzymatic preparation of fructooligosaccharides-rich burdock syrup with enhanced antioxidative properties
Fonte: Electron. j. biotechnol;40:71-77, July. 2019. tab, graf, ilus.
Idioma: en.
Projeto: Intergovernmental International Scientific and Technological Innovation Cooperation program; . Raising Program of Innovation Team for Tianjin Colleges and Universities, Tianjin, China.
Resumo: Background: Burdock (Arctium lappa L.) is a fructan-rich plant with prebiotic potential. The aim of this study was to develop an efficient enzymatic route to prepare fructooligosaccharides (FOS)-rich and highly antioxidative syrup using burdock root as a raw material. Results: Endo-inulinase significantly improved the yield of FOS 2.4-fold while tannase pretreatment further increased the yield of FOS 2.8-fold. Other enzymes, including endo-polygalacturonase, endo-glucanase and endo-xylanase, were able to increase the yield of total soluble sugar by 11.1% (w/w). By this process, a new enzymatic process for burdock syrup was developed and the yield of burdock syrup increased by 25% (w/w), whereas with FOS, total soluble sugars, total soluble protein and total soluble polyphenols were enhanced to 28.8%, 53.3%, 8.9% and 3.3% (w/w), respectively. Additionally, the scavenging abilities of DPPH and hydroxyl radicals, and total antioxidant capacity of the syrup were increased by 23.7%, 51.8% and 35.4%, respectively. Conclusions: Our results could be applied to the development of efficient extraction of valuable products from agricultural materials using enzyme-mediated methods.
Descritores: Oligossacarídeos/química
Raízes de Plantas/química
Frutose/química
Glicosídeo Hidrolases/metabolismo
Antioxidantes/química
-Oligossacarídeos/metabolismo
Poligalacturonase/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Cromatografia Líquida de Alta Pressão
Radical Hidroxila
Arctium
Alimento Funcional
Polifenóis
Frutose/metabolismo
Antioxidantes/metabolismo
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-948471
Autor: Bittar, Ingrid Mara Bicalho; Ferreira, Adão de Siqueira; Corrêa, Gilberto Fernandes.
Título: Influência da textura do solo na atividade microbiana, decomposição e mineralização do carbono de serapilheira de sítios do bioma cerrado sob condições de incubação / Influence of soil texture on microbial activity, carbon decomposition and mineralization of litter in soils of the brazilian cerrado under incubation
Fonte: Biosci. j. (Online);29(6):1952-1960, nov./dec. 2013. tab, graf.
Idioma: pt.
Resumo: A decomposição e mineralização da serapilheira são processos de fundamental importância no funcionamento do cerrado. Objetivou-se verificar a atividade microbiana e o potencial de decomposição e mineralização da serapilheira de vegetação de cerradão em solos de quatro classes texturais. As amostras foram coletadas na camada de 0- 10 cm de profundidade em quatro sítios de cerrado em solos classificados como Latossolo Amarelo distrófico típico (LAd), Latossolo Vermelho distroférrico típico (LVdf), Neossolo Quartzarênico órtico típico (RQo) e Latossolo Amarelo ácrico típico (LAw), apresentando textura média, muito argilosa, arenosa e muito argilosa, respectivamente. Quantidades de 0, 0,1, 1,0 e 10 % de resíduo de serapilheira foram adicionadas em 100 g de amostras de solo e incubados por 10 dias a 25 oC. No ensaio, foram realizadas as seguintes análises: atividade microbiana (liberação de CO2), carbono orgânico total no início e final do ensaio, atividade de ß-glicosidase e urease. A atividade microbiana aumentou significativamente com adição de 1 e 10% de resíduo da serapilheira em relação ao controle, sendo que adição de 0,1 % não mostrou diferença para o controle. O solo RQo apresentou maior atividade quando adicionado 10% de resíduo de serapilheira em relação aos demais solos. A ordem de mineralização do carbono orgânico foi LVdf > LAw > LAd > RQo, mostrando que os solos de textura muito argilosa apresentaram maior porcentagem de mineralização. A atividade de ß-glicosidase aumentou significativamente com adição de apenas 10% de resíduos de serapilheira em todos os sítios, sendo as maiores atividades observadas no RQo. A atividade de urease não foi alterada com a adição de resíduo de serapilheira. Porém, o LVdf apresentou aumento significativo em relação aos demais sítios estudados, sugerindo que a maior mineralização do carbono em LVdf pode estar relacionada a atividade dessa enzima. Os resultados mostram que a textura do solo pode ter implicações importantes sobre a atividade microbiana, a mineralização e a decomposição do resíduo de serapilheira em sítios do bioma cerrado.

Litter decomposition and mineralization are fundamentally important to Cerrado function. The aim of this study was to compare the soil microbial activity, potential decomposition and mineralization of savanna litter, under laboratory incubation, in soils from four textural classes. Soil samples were collected at a depth of 10 cm from four Cerrado sites and classified as Latossolo Amarelo distrófico típico (LAd), (sandy clay loam); Latossolo Vermelho distroférrico típico (LVdf), (clay); Neossolo Quartzarênico órtico típico (Rqo), (sandy) and Latosso Amarelo ácrico típico (LAw), (clay). Litter was added to 100 g soil at rates of 0, 0.1, 1.0 and 10% and incubated for 10 days at 25 oC. Soil microbial activity (CO2 release), total organic carbon (at the beginning and end of the assay), and ß-glucosidase and urease activity were measured. Relative to the control, soil microbial activity increased significantly with 1 and 10% litter. With 10% litter, microbial activity was higher in soil from RQo than in soils from the other sites. The order of organic carbon mineralization was LVdf > LAw > LAd > RQo, suggesting that clayey soils have higher mineralization rates. At all sites, ß-glucosidase activity increased significantly in response to addition of 10% litter only, and was highest in RQo. Urease activity did not respond to litter addition. However, urease activity in LVdf was significantly higher than in the other soils. The results show that soil texture may have important implications for soil microbial activity and decomposition and mineralization of savanna litter.
Descritores: Urease
Microbiologia Ambiental
Glicosídeo Hidrolases
-Pradaria
Responsável: BR396.1 - Biblioteca Central


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Id: biblio-1049184
Autor: Miguel, Divino Levi; Silva, Eliane Maria Ribeiro da; Silva, Cristiane Figueira da; Pereira, Marcos Gervasio; Leite, Luiz Fernando Carvalho.
Título: Soil microbiological properties and enzyme activity in agroforestry systems compared with monoculture, natural regeneration, and native Caatinga / Propriedades microbiológicas e atividade enzimática do solo sob sistemas agroflorestais comparado com monocultura, regeneração natural e caatinga nativa
Fonte: Biosci. j. (Online);36(1):1-16, jan./feb. 2020. tab, ilus.
Idioma: en.
Resumo: The objective of this study was to evaluate the influence of agroforestry systems of different ages (AFS1: one-year old; AFS5: five-years old) on the biological attributes of soil; the following systems were used for comparison: a slash-and-burn (SBF) farming area, Caatinga which has been undergoing regeneration for 6 years (CaR6), and native Caatinga (NCa) in Brazil. Enzyme activity, abundance and composition of arbuscular mycorrhizal fungi (AMF), and production of glomalin-related soil proteins (GRSP) were evaluated at soil depths of 0­0.05 m. AMF species composition in the AFS was more similar to that in the NCa than in the SBF and CaR6 systems. In the rainy season, sporulation was most abundant in the AFS-1, CaR6, and SBF systems, whereas GRSP concentrations were highest in the AFS5 during the dry season. Acid phosphatase and arylsulfatase enzyme activity was lower in the AFS1 soils than in the NCa and SBF soils (rainy period), and levels of ß-glucosidase and fluorescein diacetate hydrolysis in the AFS were equal to or higher than those in the NCa in the dry season but lower in the rainy season. AFS thus appear to promote the maintenance of soil biological quality, and may be more sustainable than SBF farming systems in the Brazilian Caatinga over the long term.

O objetivo do estudo foi avaliar a influência de sistemas agroflorestais (AFS1: um ano de idade; AFS5: cinco anos de idade), nos atributos biológicos do solo usando como referência, uma área de agricultura de corte e queima (SBF), Caatinga em regeneração há 6 anos (CaR6), e Caatinga nativa (NCa), in Brasil. A atividade enzimática, a abundância e composição dos fungos micorrízicos arbusculares (AMF), e a produção de proteína do solo relacionada à glomalina (GRSP) foram avaliados, na profundidade de 0-5 cm do solo. A composição das espécies de AMF nos AFS foi mais semelhante a observada na NCa, do que os sistemas SBF e CaR6. Na estação chuvosa, a esporulação foi mais abundante em AFS-1, CaR6 and SBF quando comparada as outras áreas, enquanto a GRSP apresentou maiores teores no AFS5 no período seco. AFS1 apresentou atividade da fosfatase ácida e arilsulfatase inferiores tanto a NCa quanto a SBF, no período chuvoso. No período seco, a atividade de ß-glicosidase e a hidrólise do diacetato de fluoresceína (FDA) na AFS foram iguais ou superiores a Nca, mas menor no período chuvoso. Verifica-se que os AFS são potenciais para a manutenção da qualidade biológica do solo, podendo, em longo prazo, serem mais sustentáveis que a SBF, em ambiente de Caatinga.
Descritores: Arilsulfatases
Solo
Fosfatase Ácida
Glicosídeo Hidrolases
Responsável: BR396.1 - Biblioteca Central


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Id: biblio-1022610
Autor: Xiao, Qiong; Zhu, Yanbing; Li, Jiajia; Wu, Changzheng; Ni, Hui; Xiao, Anfeng.
Título: Fermentation optimization and enzyme characterization of a new ι-Carrageenase from Pseudoalteromonas carrageenovora ASY5
Fonte: Electron. j. biotechnol;32:26-34, Mar. 2018. graf, tab.
Idioma: en.
Projeto: University-Enterprise Cooperation of Fujian Province; . Public Science and Technology Research Funds Projects of Ocean; . Major Science and Technology Programs and Special Topics of Fujian Province; . Key Program of Science Foundation of Fujian Province.
Resumo: Background: A new ι-carrageenase-producing strain was screened from mangroves and authenticated as Pseudoalteromonas carrageenovora ASY5 in our laboratory. The potential application of this new strain was evaluated. Results: Medium compositions and culturing conditions in shaking flask fermentation were firstly optimized by single-factor experiment. ι-Carrageenase activity increased from 0.34 U/mL to 1.08 U/mL after test optimization. Optimal fermentation conditions were 20°C, pH 7.0, incubation time of 40 h, 15 g/L NaCl, 1.5% (w/v) yeast extract as nitrogen source, and 0.9% (w/v) ι-carrageenan as carbon source. Then, the crude ι-carrageenase was characterized. The optimum temperature and pH of the ι-carrageenase were 40°C and 8.0, respectively. The enzymatic activity at 35­40°C for 45 min retained more than 40% of the maximum activity. Meanwhile, The ι-carrageenase was inhibited by the addition of 1 mmol/L Cd2+ and Fe3+ but increased by the addition of 1 mmol/L Ag+, Ba2+, Ca2+, Co2+, Mn2+, Zn2+, Fe2+, and Al3+. The structure of oligosaccharides derived from ι-carrageenan was detected using electrospray ionization mass spectrometry (ESI-MS). The ι-carrageenase degraded ι-carrageenan, yielding disaccharides and tetrasaccharides as main products. Conclusions: The discovery and study of new ι-carrageenases are beneficial not only for the production of ι-carrageenan oligosaccharides but also for the further utilization in industrial production.
Descritores: Proteínas de Bactérias/metabolismo
Pseudoalteromonas/enzimologia
Glicosídeo Hidrolases/metabolismo
-Oligossacarídeos/biossíntese
Temperatura
Carbono/metabolismo
Carragenina/biossíntese
Espectrometria de Massas por Ionização por Electrospray
Fermentação
Concentração de Íons de Hidrogênio
Hidrólise
Nitrogênio/metabolismo
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1017249
Autor: Li, Tao; Ding, Yatong; Zhang, Jun; Jiao, Guobao; Sun, Lipeng; Liu, Zhongmin; Qiu, Liyou.
Título: Improving the expression of recombinant pullulanase by increasing mRNA stability in Escherichia coli
Fonte: Electron. j. biotechnol;29:63-67, sept. 2017. ilus, tab, graf.
Idioma: en.
Projeto: National Science and Technology Program in Rural Areas during the 12th Five-Year Plan period.
Resumo: Background: Pullulanase production in both wild-type strains and recombinantly engineered strains remains low. The Shine-Dalgarno (SD) sequence and stem-loop structure in the 5' or 3' untranslated region (UTR) are well-known determinants of mRNA stability. This study investigated the effect of mRNA stability on pullulanase heterologous expression. Results: We constructed four DNA fragments, pulA, SD-pulA, pulA-3t, and SD-pulA-3t, which were cloned into the expression vector pHT43 to generate four pullulanase expression plasmids. The DNA fragment pulA was the coding sequence (CDS) of pulA in Klebsiella variicola Z-13. SD-pulA was constructed by the addition of the 5' SD sequence at the 5' UTR of pulA. pulA-3t was constructed by the addition of a 3' stem-loop structure at the 3' UTR of pulA. SD-pulA-3t was constructed by the addition of the 5' SD sequence at the 5' UTR and a 3' stem-loop structure at the 3' UTR of pulA. The four vectors were transformed into Escherichia coli BL21(DE3). The pulA mRNA transcription of the transformant harboring pHT43-SD-pulA-3t was 338.6%, 34.9%, and 79.9% higher than that of the other three transformants, whereas the fermentation enzyme activities in culture broth and intracellularly were 107.0 and 584.1 times, 1.2 and 2.0 times, and 62.0 and 531.5 times the amount of the other three transformants (pulA, SD-pulA, and pulA-3 t), respectively. Conclusion: The addition of the 5' SD sequence at the 5' UTR and a 3' stem-loop structure at the 3' UTR of the pulA gene is an effective approach to increase pulA gene expression and fermentation enzyme activity.
Descritores: Escherichia coli/enzimologia
Escherichia coli/genética
Glicosídeo Hidrolases/metabolismo
-Transformação Genética
Expressão Gênica
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Estabilidade de RNA
Fermentação
Vetores Genéticos
Glicosídeo Hidrolases/genética
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1009650
Autor: Niu, Dandan; Qiao, Jian; Li, Pujun; Tian, Kangming; Liu, Xiaoguang; Singh, Suren; Lu, Fuping.
Título: Highly efficient enzymatic preparation of isomalto-oligosaccharides from starch using an enzyme cocktail
Fonte: Electron. j. biotechnol;26:46-51, Mar. 2017. graf, tab.
Idioma: en.
Projeto: Tianjin Research Program of Application Foundation and Advanced Technology; . Science and Technology Development Foundation of Fujian Higher Education; . Priming Scientific Research Foundation of Fuzhou University; . Science and Technology Development Foundation of Tianjin Higher Education; . National Natural Science Foundation of China.
Resumo: Background: Current commercial production of isomalto-oligosaccharides (IMOs) commonly involves a lengthy multistage process with low yields. Results: To improve the process efficiency for production of IMOs, we developed a simple and efficient method by using enzyme cocktails composed of the recombinant Bacillus naganoensis pullulanase produced by Bacillus licheniformis, α-amylase from Bacillus amyloliquefaciens, barley bran ß-amylase, and α-transglucosidase from Aspergillus niger to perform simultaneous saccharification and transglycosylation to process the liquefied starch. After 13 h of reacting time, 49.09% IMOs (calculated from the total amount of isomaltose, isomaltotriose, and panose) were produced. Conclusions: Our method of using an enzyme cocktail for the efficient production of IMOs offers an attractive alternative to the process presently in use.
Descritores: Oligossacarídeos/metabolismo
Amido/metabolismo
Enzimas/metabolismo
Isomaltose/metabolismo
-Oligossacarídeos/biossíntese
Aspergillus niger/enzimologia
Temperatura
Bacillus/enzimologia
beta-Amilase/metabolismo
Glicosilação
Liquefação
alfa-Amilases/metabolismo
Fermentação
Glucosidases/metabolismo
Glicosídeo Hidrolases/metabolismo
Concentração de Íons de Hidrogênio
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1008291
Autor: Xiao, Anfeng; Xiao, Qiong; Lin, Yan; Ni, Hui; Zhu, Yanbing; Cai, Huinong.
Título: Efficient immobilization of agarase using carboxyl-functionalized magnetic nanoparticles as support
Fonte: Electron. j. biotechnol;25:13-20, ene. 2017. ilus, graf.
Idioma: en.
Projeto: University-Enterprise Cooperation of Fujian Province University; . Major Science and Technology Programs and Special Topics of Fujian Province.
Resumo: Background: A simple and efficient strategy for agarase immobilization was developed with carboxyl-functionalized magnetic nanoparticles (CMNPs) as support. The CMNPs and immobilized agarase (agarase-CMNPs) were characterized by transmission electron microscopy, dynamic light scattering, vibrating sample magnetometry, scanning electron microscopy, X-ray diffraction, thermogravimetric analysis, and zeta-potential analysis. The hydrolyzed products were separated and detected by ESI-TOF-MS. Results: The agarase-CMNPs exhibited a regular spherical shape with a mean diameter of 12 nm, whereas their average size in the aqueous solution was 43.7 nm as measured by dynamic light scattering. These results indicated that agarase-CMNPs had water swelling properties. Saturation magnetizations were 44 and 29 emu/g for the carriers and agarase-CMNPs, respectively. Thus, the particles had superparamagnetic characteristics, and agarase was successfully immobilized onto the supports. Agaro-oligosaccharides were prepared with agar as substrate using agarase-CMNPs as biocatalyst. The catalytic activity of agarase-CMNPs was unchanged after six reuses. The ESI-TOF mass spectrogram showed that the major products hydrolyzed by agarase-CMNPs after six recycle uses were neoagarotetraose, neoagarohexaose, and neoagarooctaose. Meanwhile, the end-products after 90 min of enzymatic treatment by agarase-CMNPs were neoagarobiose and neoagarotetraose. Conclusions: The enhanced agarase properties upon immobilization suggested that CMNPs can be effective carriers for agarase immobilization. Agarase-CMNPs can be remarkably used in developing systems for repeated batch production of agar-derived oligosaccharides.
Descritores: Oligossacarídeos/metabolismo
Enzimas Imobilizadas
Nanopartículas de Magnetita/química
Glicosídeo Hidrolases/metabolismo
-Termogravimetria
Difração de Raios X
Estabilidade Enzimática
Catálise
Microscopia Eletrônica de Transmissão
Magnetometria
Difusão Dinâmica da Luz
Glicosídeo Hidrolases/química
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-967017
Autor: Khalili, Elham; Huyop, Fahrul; Javed, Muhammad Arshad; Mahat, Naji Arafat; Batumalaie, Kalaivani; Wahab, Roswanira Abdul.
Título: Assessments on the catalytic and kinetic properties of beta-glucosidase isolated from a highly efficient antagonistic fungus Trichoderma harzianum / Avaliações das propriedades catalíticas e cinéticas da beta-glucosidase isoladas de um fungo antagonísta altamente eficiente Trichoderma harzianum
Fonte: Biosci. j. (Online);34(4):830-847, july/aug. 2018. tab, ilus, graf.
Idioma: en.
Resumo: Due to the toxicity and inefficiency of chemical fungicides to control infestation of Macrophomina phaseolina (Tassi) Goid which causes charcoal rot in plants, a biotechnological approach using - glucosidase (EC.3.2.1) as the alternative bioactive ingredient in fungicide is hereby, proposed. The extracellular enzyme was isolated from a highly efficient fungal antagonist, Trichoderma harzianum T12. The highly similar molecular masses obtained using SDS-PAGE (96 kDa) and MALDI-TOF mass spectrometry (98.3 kDa) affirmed that the -glucosidase was purified to homogeneity. Consequently, optimum catalytic parameters that rendered the highest enzyme activity were found to be: 45°C, pH 7, inoculum size of 10 % (w/v), supplementation with metal ions Zn2+ and Mn2+ ions, and Tween 80. Addition of wheat bran and (NH4)2SO4 as carbon and nitrogen sources also improved enzyme activity. BLASTn showed the sequence of -glucosidase T12 was highly identical to other -glucosidases viz. T. harzianum strain IOC-3844 (99%), T. gamsii and T. virens bgl1 (86 %) as well as T. reesei strain SJVTR and T. viride strain AS 3.3711 (84 %). Kinetic assessment showed that -glucosidase T12 catalyzes hydrolytic activity is characterized by a Km of 0.79 mM and Vmax of 8.45 mM min-1 mg-1 protein, with a corresponding kcat of 10.69 s-1.

Devido à toxicidade e ineficiência dos fungicidas químicos para controlar a infestação de Macrophomina phaseolina (Tassi) Goid que causa o apodrecimento das plantas, uma abordagem biotecnológica usando - glicosidase (EC.3.2.1) como o ingrediente bioativo alternativo do fungicida é por este meio, proposto. A enzima extracelular foi isolada de um antagonista fúngico altamente eficiente, o Trichoderma harzianum T12. As massas moleculares altamente similares obtidas usando SDS-PAGE (96 kDa) e espectrometria de massa MALDI-TOF (98,3 kDa) afirmaram que a -glicosidase foi purificada até a homogeneidade. Consequentemente, os parâmetros catalíticos ótimos que apresentaram a maior atividade enzimática foram: 45°C, pH 7, tamanho do inóculo de 10% (p / v), suplementação com íons de metais Zn2+ e Mn2+, e Tween 80. Adição de farelo de trigo e (NH4) 2SO4 como fontes de carbono e nitrogênio também melhoraram a atividade enzimática. O BLASTn mostrou que a sequência da -glicosidase T12 era altamente idêntica a outras -glicosidase viz. A estirpe T. harzianum IOC-3844 (99%), T. gamsii e T. virens bgl1 (86%) assim como a estirpe T. reesei SJVTR e a estirpe T. viride AS 3.3711 (84%). A avaliação cinética mostrou que -glicosidase T12 catalisa a actividade hidrolítica caracterizada por um Km de 0,79 mM e Vmax de 8,45 mM min-1 mg-1 de proteína, com um correspondente kcat de 10,69 s-1.
Descritores: Trichoderma
Cinética
Fungos
Fungicidas Industriais
Glicosídeo Hidrolases
-Biotecnologia
Responsável: BR396.1 - Biblioteca Central


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Id: biblio-889174
Autor: Melo, Ricardo Rodrigues de; Persinoti, Gabriela Felix; Paixão, Douglas Antonio Alvaredo; Squina, Fábio Márcio; Ruller, Roberto; Sato, Helia Harumi.
Título: Draft genome sequence of Streptomyces sp. strain F1, a potential source for glycoside hydrolases isolated from Brazilian soil
Fonte: Braz. j. microbiol;48(4):612-614, Oct.-Dec. 2017. tab.
Idioma: en.
Resumo: ABSTRACT Here, we show the draft genome sequence of Streptomyces sp. F1, a strain isolated from soil with great potential for secretion of hydrolytic enzymes used to deconstruct cellulosic biomass. The draft genome assembly of Streptomyces sp. strain F1 has 69 contigs with a total genome size of 8,142,296 bp and G + C 72.65%. Preliminary genome analysis identified 175 proteins as Carbohydrate-Active Enzymes, being 85 glycoside hydrolases organized in 33 distinct families. This draft genome information provides new insights on the key genes encoding hydrolytic enzymes involved in biomass deconstruction employed by soil bacteria.
Descritores: Proteínas de Bactérias/genética
Genoma Bacteriano
Glicosídeo Hidrolases/genética
Microbiologia do Solo
Streptomyces/enzimologia
Streptomyces/isolamento & purificação
-Proteínas de Bactérias/metabolismo
Composição de Bases
Brasil
Glicosídeo Hidrolases/metabolismo
Família Multigênica
Filogenia
Streptomyces/classificação
Streptomyces/genética
Responsável: BR1.1 - BIREME



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