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Id: biblio-1050037
Autor: Konar, Atheni; Sarkar, Tandra; Sukul, Nirmal Chandra; Sukul, Abirban; Chakraborty, Indrani; Ray, Sriparna.
Título: High and ultra low concentrations of Mercuric chloride initiate their specific action on binding sites of invertase and modify its interaction with sucrose
Fonte: Int. j. high dilution res;18(3/4):19-34, 2019.
Idioma: en.
Resumo: Background: Mercuric chloride is known to inhibit the activity of enzymes. It is used in homeopathy at ultra low concentration (ULC) and is known as Mercurius corrosivus (Merc cor). ULCs of Merc cor are reported to promote enzyme activity. Objective: To see whether the mother tincture (θ) of Merc cor and its ULCs interact with an enzyme invertase at its binding sites and influence enzyme's action on its substrate sucrose. Methods: Merc cor θ (0.15 M HgCl2) was diluted with deionized and distilled (DD) water 1:100 and succussed 10 times to prepare Merc cor 1 cH or 1st potency. This potency was further diluted and succussed in 200 and 1000 steps to prepare 200cH and 1000cH potencies, respectively. Merc cor 200 cH and 1000cH were prepared in 90% ethanol. The two potencies and blank 90% EtOH were diluted with DD water 1:1000 to minimize ethanol content to a negligible amount 0.09%. The control was DD water (0.99g/M). The drugs, EtOH and water control were mixed separately with 0.037 mM invertase in DD water. Using an isothermal calorimetry (ITC) instrument the substrate sucrose (65mM) was injected at 2 µl every 2 min into 300 µl invertase solution 20 times at 25 0C. Molecular modeling study was done to predict possible binding sites and nature of binding between the enzyme and HgCl2, and between the enzyme and water. Potencies after dilution are virtually water. Fluorescence spectra of invertase (4µM) mixed with drug/control solutions were also obtained to see the effect of drugs on protein folding. Results: Thermodynamic parameters like binding constant (K), change in enthalpy(ΔH), entropy(ΔS) and Gibbs free energy(ΔG) showed marked variation in treatment effects on the enzyme. Molecular modeling study also shows variation in binding between invertase and HgCl2, and between invertase and water. Fluorescence spectra show variation in quenching related to different treatments. Conclusion: Merc cor mother tincture and its potencies interact at different binding sites of invertase and modify the enzyme's action on sucrose. So, potencies act as modulators of ligand, sucrose. Drug solutions induce conformational changes in the enzyme. (au)
Descritores: Sacarose
Sítios de Ligação
Modelos Moleculares
Baixas Potências
beta-Frutofuranosidase
Homeopatia
Cloreto de Mercúrio
Responsável: BR926.1 - Biblioteca Artur de Almeida Rezende Filho


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Id: biblio-963875
Autor: Fuzhao, Nian; Leifeng, Zhao.
Título: Molecular characterization and expression pattern of tobacco (Nicotiana tabacum) apoplastic invertase gene / Caracterização molecular e padrão de expressão do gene da invertase do apoplasto em Nicotiana tabacum
Fonte: Biosci. j. (Online);31(3):730-736, may./jun. 2015.
Idioma: en.
Resumo: The complete mRNA sequence of one tobacco (Nicotiana tabacum) gene- apoplastic invertase, was amplified using the rapid amplification of cDNA ends methods based on some tobacco ESTs. The full-length tobacco apoplastic invertase gene mRNA was 1,985bp containing an 1,740 bp open reading frame, which encodes a protein of 579 amino acids. Sequence analysis revealed that the apoplastic invertase of tobacco shares high homology with the apoplastic invertase of potato (82%), Lycopersicon esculentum (81%) and Lycopersicon pennellii (78%). Results also showed that tobacco apoplastic invertase gene has a closer genetic relationship with the apoplastic invertase gene of Lycopersicon esculentum. The prediction of transmembrane helices showed that tobacco apoplastic invertase might be a transmembrane protein. The expression profile was studied and the results indicated that tobacco apoplastic invertase gene was differentially expressed in detected tobacco tissues including leaf, stem, root and flower. Our experiment established the foundation for further research on this tobacco gene.

A sequência complete do mRNA em fumo (Nicotiana tabacum) do gene da invertase apoplástica que foi amplificado usando a amplificação rápida da sua terminação pelo método usando cDNA. A sequência completa do mRNA foi de 1.985bp compreendo uma ORF ("open reading frame") de 1.740 pb que codificou 579 aminoácidos. Foi demonstrado uma homologia de 82 % nas sequências obtidas com a invertase apoplástica da batateira, 81 % com o tomateiro da espécie Lycopersicon esculentum e 78 % com Lycopersicon pennellii. Os resultados demonstraram uma homologia e relacionamento genético entre as espécies estudadas.A análise das hélices das transmembranas da invertase do apoplasto demosntraram que a mesma pode ser uma proteína da transmembrana. O padrão da expressão gênica estudado indicou que a invertase apoplástica dos tecidos do fumo incluindo, folha, caule, raiz e flor foi diferente. Novas pesquisas serão realizadas deste gene do fumo bem como sua fundamentação biológica.
Descritores: Tabaco
RNA Mensageiro
beta-Frutofuranosidase
Responsável: BR396.1 - Biblioteca Central


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Id: biblio-889130
Autor: Dinarvand, Mojdeh; Rezaee, Malahat; Foroughi, Majid.
Título: Optimizing culture conditions for production of intra and extracellular inulinase and invertase from Aspergillus niger ATCC 20611 by response surface methodology (RSM)
Fonte: Braz. j. microbiol;48(3):427-441, July-Sept. 2017. tab, graf.
Idioma: en.
Resumo: Abstract The aim of this study was obtain a model that maximizes growth and production of inulinase and invertase by Aspergillus niger ATCC 20611, employing response surface methodology (RSM). The RSM with a five-variable and three-level central composite design (CCD) was employed to optimize the medium composition. Results showed that the experimental data could be appropriately fitted into a second-order polynomial model with a coefficient of determination (R2) more than 0.90 for all responses. This model adequately explained the data variation and represented the actual relationships between the parameters and responses. The pH and temperature value of the cultivation medium were the most significant variables and the effects of inoculum size and agitation speed were slightly lower. The intra-extracellular inulinase, invertase production and biomass content increased 10-32 fold in the optimized medium condition (pH 6.5, temperature 30 °C, 6% (v/v), inoculum size and 150 rpm agitation speed) by RSM compared with medium optimized through the one-factor-at-a-time method. The process development and intensification for simultaneous production of intra-extracellular inulinase (exo and endo inulinase) and invertase from A. niger could be used for industrial applications.
Descritores: Aspergillus niger/metabolismo
beta-Frutofuranosidase/biossíntese
Glicosídeo Hidrolases/biossíntese
Microbiologia Industrial/métodos
-Aspergillus niger/enzimologia
Aspergillus niger/genética
Aspergillus niger/crescimento & desenvolvimento
beta-Frutofuranosidase/genética
Reatores Biológicos/microbiologia
Meios de Cultura/química
Meios de Cultura/metabolismo
Fermentação
Glicosídeo Hidrolases/genética
Temperatura
Tipo de Publ: Estudo de Avaliação
Responsável: BR1.1 - BIREME


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Id: biblio-884081
Autor: Agopian, Roberta Ghedini Der.
Título: Ocorrência e biossíntese de frutooligossacarídeos em banana / Occurrence and biosynthesis of fructooligosaccharides in banana.
Fonte: São Paulo; s.n; 2009. 112 p. tab, graf.
Idioma: pt.
Tese: Apresentada a Universidade de São Paulo. Faculdade de Ciências Farmacêuticas para obtenção do grau de Doutor.
Resumo: A banana tem sido comumente indicada como uma boa fonte de frutooligossacarídeos (FOS), que são considerados componentes funcionais de alimentos. Contudo, diferenças significantes em suas quantidades têm sido referidas na literatura. Portanto, uma parte do trabalho foi destinada à identificação e quantificação de FOS durante o amadurecimento de cultivares de bananas pertencentes aos grupos genômicos mais comumente cultivados no Brasil. Considerando as diferenças de cultivar, estágio do amadurecimento e metodologia usada para análise de FOS, os conteúdos dos açúcares foram analisados por cromatografia líquida de alta performance (HPAEC-PAD) e cromatografia a gás (CG-MS). Uma pesquisa inicial entre oito cultivares no estágio maduro, mostrou acúmulo de 1-cestose, primeiro membro da série de FOS, em todas elas (quantidades entre 297 e 1600 µg/g M.S). A nistose, o segundo membro, foi detectado somente na cultivar Prata. Com bases nestes dados, foram escolhidas cinco cultivares, para que fossem analisadas durante todo o amadurecimento. Os resultados mostraram uma forte correlação entre a chegada a um nível específico de sacarose (~200 mg/g M.S) e a síntese de 1-cestose. Em uma segunda fase, os níveis de sacarose e FOS total foram quantificados em diferentes fases de amadurecimento de banana Prata, armazenada em temperatura ambiente e em baixa temperatura. As supostas enzimas envolvidas em sua síntese também foram avaliadas. Para explorar a possibilidade da invertase ser responsável pela atividade de frutosiltransferase em banana, foi medido o efeito do inibidor Piridoxal HCl, os níveis de concentração do substrato e as atividades de hidrólise e transglicosilação, e o efeito do tempo no estudo cinético da enzima. A baixa temperatura atrasou todos os eventos analisados por 15 dias e os níveis de sacarose tiveram um pequeno aumento, porém constante, enquanto a banana estava armazenada ao frio, e uma rápida elevação no final do amadurecimento. Foi detectado FOS total desde o primeiro dia pós-colheita, enquanto que a 1-cestose permaneceu indetectável até os níveis de sacarose atingirem aproximadamente 200 mg/g M.S., em ambos os grupos. Os níveis de sacarose e FOS total foram ligeiramente maiores em bananas armazenadas em baixas temperaturas do que em frutos controle. Em ambas as amostras os níveis de FOS total foram maiores que de 1-cestose. Os perfis de carboidratos por HPLC e TLC sugeriram a presença de neocestose, 6-cestose e bifurcose. A enzima supostamente responsável pela atividade de transglicosilação em banana parece ser a invertase. Contudo, os altos níveis de sacarose encontrados em banana armazenadas em baixa temperatura, poderiam ser resultado de várias mudanças de enzimas degradativas e biossíntéticas, como sacarose-sintase (SuSy), sacarose-fosfato-sintase (SPS), invertase e outras, uma vez que a sacarose possui um papel central, direta ou indiretamente, em diversas vias do metabolismo de carboidrato em banana. Assim, na última parte do trabalho foram analisados o acúmulo de sacarose e a síntese e atividade de enzimas sintéticas, hidrolíticas e fosforolíticas, importantes no metabolismo de amido-sacarose, durante o amadurecimento de banana Prata nos dois tratamentos. A baixa temperatura não danificou os frutos, aumentando a vida de prateleira deles. As amostras do frio apresentaram pequeno aumento no nível de degradação de amido e um acréscimo de 20 % na sacarose acumulada durante o amadurecimento. Foi verificado o atraso na produção de etileno, CO2, e no início de degradação de amido durante o acondicionamento ao frio, concomitante ao atraso no pico de atividade de α-amilase. O atraso no climatério também manteve alta a atividade e síntese protéica de SuSy durante o armazenamento a frio, que declinaram após a retirada do frio, como no controle. As enzimas ß-amilase, fosforilase (forma citosólica e plastidial) e SPS reagiram positivamente, sofrendo uma indução positiva na síntese e atividade enzimática durante o armazenamento ao frio, que poderia ser parte do mecanismo necessário para os maiores níveis de açúcares e para o processo de tolerância do fruto à baixa temperatura

Banana has been currently indicated as a good source of fructooligosaccharides (FOS), which are considered to be functional components of foods. However, significant differences in their amounts in bananas have been observed in the literature. So, a part of this work aims to identify and quantify FOS during ripening in different banana cultivars belonging to the most common genomic groups cultivated in Brazil. Considering that these differences can be due to cultivar, stage of ripening, and the methodologies used for FOS analyses, sugar contents were analyzed by high performance anion exchange chromatography pulsed amperiometric detection (HPAEC-PAD) and gas chromatography- mass spectrometry (GC-MS). An initial screening of eight cultivars in a full-ripe stage showed that 1-Kestose, the first member of the FOS series (amounts between 297 and 1600 µg/g of D.M), was accumulated in all of them. Nystose, the second member, was detected only in Prata cultivar. Five of the cultivars were analyzed during ripening, and a strong correlation could be established with a specific sucrose level (~200 mg/g of D.M.), which seems to trigger the synthesis of 1-Kestose. In a second part of this work, the levels of sucrose and total-FOS were quantified in different phases of banana Prata ripening stored at ambient and low temperature. The supposed enzymes involved in their synthesis were also evaluated. To explore the possibility that invertase could be responsible for the fructosyltransferase activity in banana, we measured the effect of the inhibitor Pyridoxal HCl, the level of substrate concentration on both hydrolyze and transglycosylase activity in the same protein extract and the effect of time on kinetic study of the enzyme. The cold temperature delayed all the analyzed events for 15 days and sucrose levels increased low, but constantly, while banana were stored at low temperature and had a burst when it increased. Total-FOS were detected in the first days after harvest, while 1-kestose remained undetectable until the sucrose levels were around 200 mg.g (dry weight), in both groups. Total-FOS and sucrose levels were higher in banana stored at low temperature than in control. In both samples total-FOS levels were higher than 1-kestose. The carbohydrate profiles by HPLC and TLC suggest the presence of neokestose, 6-kestose and bifurcose. The enzyme supposed to be responsible for the transglycosilation activity in banana, seems to be an invertase. However, the higher sucrose levels found in banana stored at low temperature could be result of several changes in biosynthetic and degradative enzymes, such sucrose-synthase, sucrose-phosphate-synthase, invertase and others, once that sucrose plays a central role in a lot of direct and indirect carbohydrate pathways in banana fruits. So, in the last part of this work, we analyzed the sucrose accumulation and synthesis and activity of synthetic, hydrolytic and phosphorolytic enzymes that are important in the starch-sucrose metabolism during ripening of banana Prata stored at ambient and low temperature. The levels of starch degradation and sucrose accumulation (around 20% over) showed high levels in cold fruits as compared with control, during the ripening. The cold temperature delayed the ethylene and CO2 production, and the beginning of the starch degradation, concomitantly with a delay in the profile of α-amylase synthesis and activity. The late climateric also maintained the high synthesis and activity of SuSy during the cold storage that decreased just after ending the cold exposure. The ß-amylase, phosphorylase (plastidial and citossolic forms) and the SPS enzymes showed a positive induction in the both activity and synthesis of protein during the cold storage. It could be important to the higher sugars levels showed at low temperature and that could contribute to the process of cold resistance in banana fruit
Descritores: Musa/genética
Biossíntese de Proteínas
Sacarose
-beta-Frutofuranosidase
Cromatografia Gasosa
Cromatografia Líquida de Alta Pressão/métodos
Frutanos
Responsável: BR40.1 - DBD - Divisão de Biblioteca e Documentacão do Conjunto das Químicas


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Id: lil-775098
Autor: Ali, Sikander; Aslam, Aafia; Hayyat, Muhammad Umar.
Título: Double mutation of Saccharomyces cerevisiae for enhanced β-D-fructofuranosidase fructohydrolase productivity and application of growth kinetics for parametric significance analysis
Fonte: Braz. j. microbiol;47(1):136-142, Jan.-Mar. 2016. tab, graf.
Idioma: en.
Resumo: Abstract The kinetics of an extracellular β-D-fructofuranosidase fructohydrolase production by Saccharomyces cerevisiae in a chemically defined medium, i.e., sucrose peptone agar yeast extract at pH 6, was investigated. The wild-type was treated with a chemical mutagen, methyl methane sulfonate. Among the six mutants isolated, methyl methane sulfonate-V was found to be a better enzyme producing strain (52 ± 2.4a U/mL). The maximum production (74 ± 3.1a U/mL) was accomplished after at 48 h (68 ± 2.7a mg/mL protein). The mutants were stabilized at low levels of 5-fluoro-cytocine and the viable ones were further processed for optimization of cultural conditions and nutritional requirements. The sucrose concentration, incubation period and pH were optimized to be 30 g/L, 28 °C, and 6.5, respectively. The methyl methane sulfonate-V exhibited an improvement of over 10 folds in enzyme production when 5 g/L ammonium sulfate was used as a nitrogen source. Thin layer chromatography and high-performance liquid chromatography analysis illustrated the optimal enzyme activity supported by the higher rate of hydrolysis of sucrose into monosaccharides, particularly α-D-glucose and β-D-fructose. The values for Qp (2 ± 0.12c U/mL/h) and Yp/s (4 ± 1.24b U/g) of the mutant were considerably increased in comparison with other yeast strains (both isolates and viable mutants). The mutant could be exploited for enzyme production over a wider temperature range (26–34 °C), with significantly high enzyme activity (LSD 0.048, HS) at the optimal temperature.
Descritores: Mutação
Saccharomyces cerevisiae/crescimento & desenvolvimento
Saccharomyces cerevisiae/metabolismo
beta-Frutofuranosidase/biossíntese
-Cromatografia Líquida de Alta Pressão
Cromatografia em Camada Delgada
Meios de Cultura/química
Concentração de Íons de Hidrogênio
Hidrólise
Mutagênese
Mutagênicos/metabolismo
Serratia
Saccharomyces cerevisiae/genética
Sacarose/metabolismo
Ácidos Sulfínicos/metabolismo
Temperatura
Responsável: BR1.1 - BIREME


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Id: lil-723091
Autor: Veana, F.; Martínez-Hernández, J.L.; Aguilar, C.N.; Rodríguez-Herrera, R.; Michelena, G..
Título: Utilization of molasses and sugar cane bagasse for production of fungal invertase in solid state fermentation using Aspergillus niger GH1
Fonte: Braz. j. microbiol;45(2):373-377, Apr.-June 2014. graf, tab.
Idioma: en.
Resumo: Agro-industrial wastes have been used as substrate-support in solid state fermentation for enzyme production. Molasses and sugarcane bagasse are by-products of sugar industry and can be employed as substrates for invertase production. Invertase is an important enzyme for sweeteners development. In this study, a xerophilic fungus Aspergillus niger GH1 isolated of the Mexican semi-desert, previously reported as an invertase over-producer strain was used. Molasses from Mexico and Cuba were chemically analyzed (total and reducer sugars, nitrogen and phosphorous contents); the last one was selected based on chemical composition. Fermentations were performed using virgin and hydrolyzate bagasse (treatment with concentrated sulfuric acid). Results indicated that, the enzymatic yield (5231 U/L) is higher than those reported by other A. niger strains under solid state fermentation, using hydrolyzate bagasse. The acid hydrolysis promotes availability of fermentable sugars. In addition, maximum invertase activity was detected at 24 h using low substrate concentration, which may reduce production costs. This study presents an alternative method for invertase production using a xerophilic fungus isolated from Mexican semi-desert and inexpensive substrates (molasses and sugarcane bagasse).
Descritores: Aspergillus niger/crescimento & desenvolvimento
Aspergillus niger/metabolismo
Melaço
Saccharum/metabolismo
Resíduos
beta-Frutofuranosidase/isolamento & purificação
beta-Frutofuranosidase/metabolismo
-Aspergillus niger/isolamento & purificação
Cuba
Carboidratos/análise
Fermentação
México
Nitrogênio/análise
Fósforo/análise
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: lil-591932
Autor: Rustiguel, Cynthia Barbosa; Oliveira, Arthur Henrique Cavalcanti de; Terenzi, Héctor Francisco; Jorge, João Atílio; Guimarães, Luis Henrique Souza.
Título: Biochemical properties of an extracellular beta-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate
Fonte: Electron. j. biotechnol;14(2):2-2, Mar. 2011. ilus, tab.
Idioma: en.
Resumo: The filamentous fungus A. phoenicis produced high levels of beta-D-fructofuranosidase (FFase) when grown for 72 hrs under Solid-State Fermentation (SSF), using soy bran moistened with tap water (1:0.5 w/v) as substrate/carbon source. Two isoforms (I and II) were obtained, and FFase II was purified 18-fold to apparent homogeneity with 14 percent recovery. The native molecular mass of the glycoprotein (12 percent of carbohydrate content) was 158.5 kDa with two subunits of 85 kDa estimated by SDS-PAGE. Optima of temperature and pH were 55ºC and 4.5. The enzyme was stable for more than 1 hr at 50ºC and was also stable in a pH range from 7.0 to 8.0. FFase II retained 80 percent of activity after storage at 4ºC by 200 hrs. Dichroism analysis showed the presence of random and beta-sheet structure. A. phoenicis FFase II was activated by Mn2+, Mg2+ and Co2+, and inhibited by Cu2+, Hg2+ and EDTA. The enzyme hydrolyzed sucrose, inulin and raffinose. Kd and Vmax values were 18 mM and 189 U/mg protein using sucrose as substrate.
Descritores: Aspergillus/enzimologia
beta-Frutofuranosidase/metabolismo
-Estabilidade Enzimática
Concentração de Íons de Hidrogênio
Hidrólise
Microbiologia Industrial
Cinética
Substratos para Tratamento Biológico
Sacarose
Temperatura
beta-Frutofuranosidase/isolamento & purificação
Responsável: CL1.1 - Biblioteca Central


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Id: lil-448782
Autor: Almeida, Ana Cláudia Santana de; Araújo, Luciares Costa de; Costa, Andressa Mendes; Abreu, César Augusto Moraes de; Lima, Maria Alice Gomes de Andrade; Palha, Maria de Los Angeles Perez Fernandez.
Título: Sucrose hydrolysis catalyzed by auto-immobilized invertase into intact cells of Cladosporium cladosporioides
Fonte: Electron. j. biotechnol;8(1):54-62, Apr. 2005. ilus, tab, graf.
Idioma: en.
Resumo: The enzyme known as invertase (E.C. 3.2.1.26 - beta-D-fructofuranosidase) catalyzes the sucrose hydrolysis producing an equimolar mixture of glucose and fructose named inverted sugar. The fungus Cladosporium cladosporioides has invertase as its constituent. Hence, its use as a natural immobilized support for the invertase produces interesting results for the enzyme. The present work has the objective of determining the optimum operational conditions of auto-immobilized invertase, as well as its kinetic parameters (K M and Vmax). A complete 2³ factorial planning was done for the evaluation of such parameters. Temperature, pH and agitation level were the studied variables. The hydrolysis percentage was the monitored result. Batch tests in optimum conditions were done to determine the kinetic parameters. Temperature of 70ºC, pH 6 and agitation of 170 rpm were the established conditions for the hydrolysis process. The auto-immobilized invertase presented a K M of 447 mM and Vmax of 2,805 mmol/min.
Descritores: Cladosporium/enzimologia
Enzimas Imobilizadas/metabolismo
beta-Frutofuranosidase/metabolismo
-Catálise
Meios de Cultura
Concentração de Íons de Hidrogênio
Hidrólise
Cinética
Sacarose/metabolismo
Temperatura
Responsável: CL1.1 - Biblioteca Central



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