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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 Ambiente
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


  2 / 25 LILACS  
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Id: biblio-1021898
Autor: Strahsburger, Erwin; Lopez de Lacey, Ana Maria; Marotti, Ilaria; DiGioia, Diana; Biavati, Bruno; Dinelli, Giovanni.
Título: In vivo assay to identify bacteria with ß-glucosidase activity
Fonte: Electron. j. biotechnol;30:83-87, nov. 2017. graf, tab.
Idioma: en.
Projeto: University of Bologna; . Universidad Arturo Prat.
Resumo: Background: ß-Glucosidase assay is performed with purified or semipurified enzymes extracted from cell lysis. However, in screening studies, to find bacteria with ß-glucosidase activity among many tested bacteria, a fast method without cell lysis is desirable. In that objective, we report an in vivo ß-glucosidase assay as a fast method to find a ß-glucosidase producer strain. Results: The method consists in growing the strains for testing in a medium supplemented with the artificial substrate p-nitrophenyl-ß-glucopyranoside (pNPG). The presence of ß-glucosidases converts the substrate to p-nitrophenol (pNP), a molecule that can be easily measured in the supernatant spectrophotometrically at 405 nm. The assay was evaluated using two Bifidobacterium strains: Bifidobacterium longum B7254 strain that lacks ß-glucosidase activity and Bifidobacterium pseudocatenulatum B7003 strain that shows ß-glucosidase activity. The addition of sodium carbonate during pNP measurement increases the sensitivity of pNP detection and avoids the masking of absorbance by the culture medium. Furthermore, we show that pNP is a stable enzymatic product, not metabolized by bacteria, but with an inhibitory effect on cell growth. The ß-glucosidase activity was measured as units of enzyme per gram per minute per dry cell weight. This method also allowed the identification of Lactobacillus strains with higher ß-glucosidase activity among several lactobacillus species. Conclusion: This in vivo ß-glucosidase assay can be used as an enzymatic test on living cells without cell disruption. The method is simple, quantitative, and recommended, especially in studies screening for bacteria not only with ß-glucosidase activity but also with high ß-glucosidase activity.
Descritores: Bifidobacterium/isolamento & purificação
Bifidobacterium/enzimologia
beta-Glucosidase/metabolismo
-Bifidobacterium/metabolismo
Nitrofenilgalactosídeos
Ensaios Enzimáticos
Bifidobacterium longum/isolamento & purificação
Bifidobacterium longum/enzimologia
Bifidobacterium pseudocatenulatum/isolamento & purificação
Bifidobacterium pseudocatenulatum/enzimologia
Lactobacillus/isolamento & purificação
Lactobacillus/enzimologia
Lactobacillus/metabolismo
Nitrofenóis
Responsável: CL1.1 - Biblioteca Central


  3 / 25 LILACS  
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Id: biblio-1009753
Autor: Song, Xiaolin; Wu, Hao; Piao, Xuanchun; Yin, Zhenhao; Yin, Chengri.
Título: Microbial transformation of ginsenosides extracted from Panax ginseng adventitious roots in an airlift bioreactor
Fonte: Electron. j. biotechnol;26:20-26, Mar. 2017. ilus, graf, tab.
Idioma: en.
Projeto: National Natural Science Foundation of China; . Natural Science Foundation of Jilin Province of China.
Resumo: Background: Ginsenoside is the most important secondary metabolite in ginseng. Natural sources of wild ginseng have been overexploited. Although root culture can reduce the length of the growth cycle of ginseng, the number of species of ginsenosides is reduced and their contents are lower in the adventitious roots of ginseng than in the roots of ginseng cultivated in the field. Results: In this study, 147 strains of ß-glucosidase-producing microorganisms were isolated from soil. Of these, strain K35 showed excellent activity for converting major ginsenosides into rare ginsenosides, and a NCBI BLAST of its 16S rDNA gene sequence showed that it was most closely related to Penicillium sp. (HQ608083.1). Strain K35 was used to ferment the adventitious root extract, and the fermentation products were analyzed by high-performance liquid chromatography. The results showed that the content of the rare ginsenoside CK was 0.253 mg mL-1 under the optimal converting conditions of 9 d of fermentation at pH 7.0 in LL medium, which was significantly higher than that in the adventitious roots of ginseng. Conclusion: These findings may not only solve the problem of low productivity of metabolite in ginseng root culture but may also result in the development of a new valuable method of manufacturing ginsenoside CK.
Descritores: beta-Glucosidase/metabolismo
Raízes de Plantas/metabolismo
Ginsenosídeos/metabolismo
Panax/metabolismo
-Penicillium
Biotransformação
Cromatografia Líquida de Alta Pressão
Raízes de Plantas/química
Reatores Biológicos
Ginsenosídeos/isolamento & purificação
Fermentação
Panax/crescimento & desenvolvimento
Panax/química
Responsável: CL1.1 - Biblioteca Central


  4 / 25 LILACS  
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Id: biblio-833321
Autor: Peru. Ministerio de Salud. Seguro Integral de Salud.
Título: Informe de evaluación rápida de tecnología sobre seguridad y efectividad de la imiglucerasa para enfermedad de Gaucher tipo I / Rapid evaluation report of technology on the safety and effectiveness of imiglucerase for Gaucher disease type I.
Fonte: s.l; s.n; 2013. tab.
Idioma: es.
Resumo: La Enfermedad de Gaucher es la enfermedad más común de depósito lisosomal, pertenece al grupo de enfermedades catalogadas como errores innatos del metabolismo y se trasmite por herencia autosómica recesiva. (1) Se caracteriza por la presencia de mutaciones patológicas en los genes que codifican la enzima ß- glucosidasa-ácida lisosomal produciendo su deficiencia parcial o total, lo que origina depósitos anormales de material glicolípido (glucocerebrósidos) en los lisosomas de los macrófagos mononucleares de los órganos ricos en células de la línea monocitosmacrófagos como el hígado, bazo, médula ósea y parénquima de los nódulos linfáticos. Se reporta después de la intervención aumento sostenido de la hemogloblina, disminución de la hepatomegalia, disminución del volumen esplénico en pacientes con esplenomeglia moderada y severa, resolución del dolor óseo, los niños que reciben la TRE pueden llegar a alcanzar la talla normal en alrededor de 3 años de tratamiento, respuesta a hipertensión pulmonar. Los pacientes con TRE tuvieron mejores puntajes para el funcionamiento físico, el rol físico, el dolor corporal, la salud general y vitalidad. Se recomienda cubrir con generación de evidencia.(AU)
Descritores: beta-Glucosidase/uso terapêutico
Doença de Gaucher/diagnóstico
Doença de Gaucher/terapia
-Avaliação da Tecnologia Biomédica
Resultado do Tratamento
Tipo de Publ: Revisão
Relatório Técnico
Estudos de Avaliação
Responsável: BR1.1 - BIREME


  5 / 25 LILACS  
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Texto completo SciELO Brasil
Texto completo
Id: lil-755814
Autor: Santos, Bruna Silveira Lamanes dos; Gomes, Arthur Filipe Sousa; Franciscon, Emanuele Giuliane; Oliveira, Jean Maikon de; Baffi, Milla Alves.
Título: Thermotolerant and mesophylic fungi from sugarcane bagasse and their prospection for biomass-degrading enzyme production
Fonte: Braz. j. microbiol;46(3):903-910, July-Sept. 2015. tab, ilus.
Idioma: en.
Resumo:

Nineteen fungi and seven yeast strains were isolated from sugarcane bagasse piles from an alcohol plant located at Brazilian Cerrado and identified up to species level on the basis of the gene sequencing of 5.8S-ITS and 26S ribosomal DNA regions. Four species were identified: Kluyveromyces marxianus, Aspergillus niger, Aspergillus sydowii and Aspergillus fumigatus, and the isolates were screened for the production of key enzymes in the saccharification of lignocellulosic material. Among them, three strains were selected as good producers of hemicellulolitic enzymes: A. niger (SBCM3), A. sydowii (SBCM7) and A. fumigatus (SBC4). The best β-xylosidase producer was A. niger SBCM3 strain. This crude enzyme presented optimal activity at pH 3.5 and 55 °C (141 U/g). For β-glucosidase and xylanase the best producer was A. fumigatus SBC4 strain, whose enzymes presented maximum activity at 60 °C and pH 3.5 (54 U/g) and 4.0 (573 U/g), respectively. All these crude enzymes presented stability around pH 3.0–8.0 and up to 60 °C, which can be very useful in industrial processes that work at high temperatures and low pHs. These enzymes also exhibited moderate tolerance to ethanol and the sugars glucose and xylose. These similar characteristics among these fungal crude enzymes suggest that they can be used synergistically in cocktails in future studies of biomass conversion with potential application in several biotechnological sectors.

.
Descritores: Aspergillus fumigatus/enzimologia
Aspergillus niger/enzimologia
Celulose/metabolismo
/metabolismo
ENDO-1,ABBREVIATIONS AS TOPIC-BETA XYLANASES/metabolismo
Kluyveromyces/enzimologia
Saccharum/microbiologia
Xilosidases/metabolismo
beta-Glucosidase/metabolismo
-Aspergillus fumigatus/isolamento & purificação
Aspergillus fumigatus/metabolismo
Aspergillus niger/isolamento & purificação
Aspergillus niger/metabolismo
Sequência de Bases
Biomassa
Brasil
DNA Fúngico/genética
DNA Intergênico/genética
Fermentação
Kluyveromyces/isolamento & purificação
Kluyveromyces/metabolismo
Lignina/metabolismo
Tipagem Molecular
Técnicas de Tipagem Micológica
RNA Ribossômico/genética
Análise de Sequência de DNA
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  6 / 25 LILACS  
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Texto completo SciELO Brasil
Texto completo
Id: lil-748234
Autor: Ahmed, Samia A.; El-Shayeb, Nefisa M.A.; Hashem, Abdel-Gawad M.; Saleh, Shireen A.A.; Abdel-Fattah, Ahmed F..
Título: Chemical modification of Aspergillus niger β-glucosidase and its catalytic properties
Fonte: Braz. j. microbiol;46(1):23-28, 05/2015. graf.
Idioma: en.
Resumo: Aspergillus niger β-glucosidase was modified by covalent coupling to periodate activated polysaccharides (glycosylation). The conjugated enzyme to activated starch showed the highest specific activity (128.5 U/mg protein). Compared to the native enzyme, the conjugated form exhibited: a higher optimal reaction temperature, a lower Ea (activation energy), a higher Km (Michaelis constant) and Vmax (maximal reaction rate), and improved thermal stability. The calculated t1/2 (half-life) values of heat in-activation at 60 °C and 70 °C were 245.7 and 54.5 min respectively, whereas at these temperatures the native enzyme was less stable (t1/2 of 200.0 and 49.5 min respectively). The conjugated enzyme retained 32.3 and 29.7%, respectively from its initial activity in presence of 5 mM Sodium Dodecyl Sulphate (SDS) and p-Chloro Mercuri Benzoate (p-CMB), while the native enzyme showed a remarkable loss of activity (retained activity 1.61 and 13.7%, respectively). The present work has established the potential of glycosylation to enhance the catalytic properties of β-glucosidase enzyme, making this enzyme potentially feasible for biotechnological applications.
Descritores: Aspergillus niger/enzimologia
beta-Glucosidase/química
beta-Glucosidase/metabolismo
-Estabilidade Enzimática
Inibidores Enzimáticos/metabolismo
Glicosilação
Cinética
Temperatura Ambiente
Responsável: BR1.1 - BIREME


  7 / 25 LILACS  
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Texto completo SciELO Brasil
Texto completo
Id: lil-741263
Autor: Harwani, Dharmesh.
Título: Regulation of gene expression: Cryptic β-glucoside (bgl) operon of Escherichia coli as a paradigm
Fonte: Braz. j. microbiol;45(4):1139-1144, Oct.-Dec. 2014. ilus.
Idioma: en.
Resumo: Bacteria have evolved various mechanisms to extract utilizable substrates from available resources and consequently acquire fitness advantage over competitors. One of the strategies is the exploitation of cryptic cellular functions encoded by genetic systems that are silent under laboratory conditions, such as the bgl (β-glucoside) operon of E. coli. The bgl operon of Escherichia coli, involved in the uptake and utilization of aromatic β-glucosides salicin and arbutin, is maintained in a silent state in the wild type organism by the presence of structural elements in the regulatory region. This operon can be activated by mutations that disrupt these negative elements. The fact that the silent bgl operon is retained without accumulating deleterious mutations seems paradoxical from an evolutionary view point. Although this operon appears to be silent, specific physiological conditions might be able to regulate its expression and/or the operon might be carrying out function(s) apart from the utilization of aromatic β-glucosides. This is consistent with the observations that the activated operon confers a Growth Advantage in Stationary Phase (GASP) phenotype to Bgl+ cells and exerts its regulation on at least twelve downstream target genes.
Descritores: Escherichia coli/enzimologia
Escherichia coli/genética
Regulação da Expressão Gênica
beta-Glucosidase/genética
beta-Glucosidase/metabolismo
-Arbutina/metabolismo
Álcoois Benzílicos/metabolismo
Escherichia coli/crescimento & desenvolvimento
Escherichia coli/metabolismo
Glucosídeos/metabolismo
Óperon
Tipo de Publ: Research Support, Non-U.S. Gov't
Revisão
Responsável: BR1.1 - BIREME


  8 / 25 LILACS  
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Texto completo SciELO Brasil
Texto completo
Id: lil-725681
Autor: Souza, Ana Maria Almeida; Muniz, Thiago Pimentel; Brito, Rafael Maciel.
Título: Study of enzyme replacement therapy for Gaucher Disease: comparative analysis of clinical and laboratory parameters at diagnosis and after two, five and ten years of treatment
Fonte: Rev. bras. hematol. hemoter;36(5):345-350, Sep-Oct/2014. tab, graf.
Idioma: en.
Resumo: Objective: To evaluate the impact of enzyme replacement therapy for Gaucher Disease on clinical and laboratory parameters after two, five and ten years of treatment. Methods: Data were collected from patient records and analyzed using BioEstat software (version 5.0). Student's t-test, Analysis of Variance (ANOVA), Wilcoxon test and Kruskal–Wallis test were used for statistical analysis. Hepatomegaly and splenomegaly were analyzed using the Kappa test. Results: There was a significant increase in hemoglobin levels (p-value <0.01) and platelet counts (p-value = 0.01) within two years of therapy. At the same time, the frequencies of splenomegaly (p-value <0.01) and hepatomegaly (p-value <0.05) reduced. These results were similar at five and ten years of enzyme replacement therapy. Conclusions: There are substantial and quick (within two years) laboratory and clinical responses to enzyme replacement therapy. These improvements continue as long as enzyme replacement therapy is administered every two weeks, as recommended by the literature...
Descritores: Anemia
Doença de Gaucher/diagnóstico
Doença de Gaucher/terapia
Terapia de Reposição de Enzimas
Esplenomegalia
-beta-Glucosidase
Sistema Fagocitário Mononuclear
Limites: Seres Humanos
Responsável: BR408.1 - Biblioteca da Faculdade de Medicina - BFM


  9 / 25 LILACS  
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Texto completo SciELO Brasil
Texto completo
Id: lil-688590
Autor: Gottschalk, Leda Maria Fortes; Paredes, Raquel de Sousa; Teixeira, Ricardo Sposina Sobral; Silva, Ayla Sant'Ana da; Bon, Elba Pinto da Silva.
Título: Efficient production of lignocellulolytic enzymes xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by the mutant strain Aspergillus awamori 2B.361 U2/1
Fonte: Braz. j. microbiol;44(2):569-576, 2013. graf, tab.
Idioma: en.
Resumo: The production of xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by Aspergillus awamori 2B.361 U2/1, a hyper producer of glucoamylase and pectinase, was evaluated using selected conditions regarding nitrogen nutrition. Submerged cultivations were carried out at 30 ºC and 200 rpm in growth media containing 30 g wheat bran/L as main carbon source and either yeast extract, ammonium sulfate, sodium nitrate or urea, as nitrogen sources; in all cases it was used a fixed molar carbon to molar nitrogen concentration of 10.3. The use of poor nitrogen sources favored the accumulation of xylanase, β-xylosidase and ferulic acid esterase to a peak concentrations of 44,880; 640 and 118 U/L, respectively, for sodium nitrate and of 34,580, 685 and 170 U/L, respectively, for urea. However, the highest β-glucosidase accumulation of 10,470 U/L was observed when the rich organic nitrogen source yeast extract was used. The maxima accumulation of filter paper activity, xylanase, β-xylosidase, ferulic acid esterase and β-glucosidase by A. awamori 2B.361 U2/1 was compared to that produced by Trichoderma reesei Rut-C30. The level of β-glucosidase was over 17-fold higher for the Aspergillus strain, whereas the levels of xylanase and β-xylosidase were over 2-fold higher. This strain also produced ferulic acid esterase (170 U/L), which was not detected in the T. reesei culture.
Descritores: Aspergillus/enzimologia
Hidrolases de Éster Carboxílico/metabolismo
Xilosidases/metabolismo
beta-Glucosidase/metabolismo
-Aspergillus/genética
Aspergillus/crescimento & desenvolvimento
Carbono/metabolismo
Meios de Cultura/química
Nitrogênio/metabolismo
Temperatura Ambiente
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


  10 / 25 LILACS  
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Texto completo SciELO Cuba
Texto completo
Id: lil-617299
Autor: Lavaut Sánchez, Kalia; Núñez Quintana, Aramís; Nordet Carreras, Ileana; González Otero, Alejandro; Svarch, Eva; Machín García, Sergio; Giraldo, Pilar; Sá Miranda, Clara.
Título: Aspectos clínicos, bioquímicos, moleculares y tratamiento de 2 pacientes con enfermedad de Gaucher / Clinical, biochemical and molecular features and the treatment of two patients presenting with Gaucher's disease
Fonte: Rev. cuba. hematol. inmunol. hemoter;26(1):54-61, ene.-mar. 2010.
Idioma: es.
Resumo: La enfermedad de Gaucher es una entidad hereditaria del metabolismo de los esfingolípidos con un patrón de herencia autosómico recesivo determinada por una deficiencia de la actividad de la enzima b-glucosidasa ácida. En este trabajo se presentan 2 pacientes en edad pediátrica, uno del sexo femenino y otro del masculino, ambos con anemia y hepatoesplenomegalia confirmadas por ultrasonido. El aspirado de médula ósea mostró infiltración por células de almacenamiento, niveles bajos de la actividad enzimática de b-glucocerebrosidasa y el diagnóstico molecular de las posibles mutaciones conocidas confirmaron la enfermedad en ambos pacientes que se encuentran en tratamiento con terapia enzimática sustitutiva (imiglucerasa), con evolución favorable en los aspectos clínicos y humorales.

Gaucher's disease is a hereditary entity related to sphingolipids metabolism with an autosomal recessive hereditary pattern determined by a failure of the acid b-glucosidase enzyme. In present paper authors present the case of two pediatric patients (1 female and 1 male) both presenting with anemia and hepatosplenomegaly by ultrasound (US). Bone marrow aspirate showed infiltration by storage cells, low levels of enzymatic activity of b-glucocerebroside and a molecular diagnosis of potential known mutations confirmed the disease in both patients, who are under treatment with substitutive enzymatic therapy (imiglucerase) with a favorable course in clinical and humoral features.
Descritores: Doença de Gaucher/terapia
Enzimas/uso terapêutico
beta-Glucosidase/deficiência
Limites: Seres Humanos
Masculino
Pré-Escolar
Criança
Feminino
Tipo de Publ: Relatos de Casos
Responsável: CU1.1 - Biblioteca Médica Nacional



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