Base de dados : LILACS
Pesquisa : G02.494 [Categoria DeCS]
Referências encontradas : 142 [refinar]
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Id: biblio-951792
Autor: Moghannem, Saad A. M; Farag, Mohamed M. S; Shehab, Amr M; Azab, Mohamed S.
Título: Exopolysaccharide production from Bacillus velezensis KY471306 using statistical experimental design
Fonte: Braz. j. microbiol;49(3):452-462, July-Sept. 2018. tab, graf.
Idioma: en.
Resumo: Abstract Exopolysaccharide (EPS) biopolymers produced by microorganisms play a crucial role in the environment such as health and bio-nanotechnology sectors, gelling agents in food and cosmetic industries in addition to bio-flocculants in the environmental sector as they are degradable, nontoxic. This study focuses on the improvement of EPS production through manipulation of different culture and environmental conditions using response surface methodology (RSM). Plackett-Burman design indicated that; molasses, yeast extract and incubation temperature are the most effective parameters. Box-Behnken RSM indicated that; the optimum concentration for each parameter was 12% (w/v) for molasses, 6 g/L yeast extract and 30 °C for incubation temperature. The most potent bacterial isolate was identified as Bacillus velezensis KY498625. After production, EPS was extracted, purified using DEAE-cellulose, identified using Fourier transform infrared (FTIR), gel permeation chromatography (GPC) and gas chromatography-mass spectroscopy (GC-MS). The result indicated that; it has molecular weight 1.14 × 105 D consisting of glucose, mannose and galactose.
Descritores: Polissacarídeos Bacterianos/metabolismo
Bacillus/metabolismo
-Polissacarídeos Bacterianos/isolamento & purificação
Polissacarídeos Bacterianos/química
Bacillus/química
Microbiologia Industrial
Espectroscopia de Infravermelho com Transformada de Fourier
Meios de Cultura/metabolismo
Meios de Cultura/química
Peso Molecular
Responsável: BR1.1 - BIREME


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Id: lil-788974
Autor: Gururaj, P; Ramalingam, Subramanian; Devi, Ganesan Nandhini; Gautam, Pennathur.
Título: Process optimization for production and purification of a thermostable, organic solvent tolerant lipase from Acinetobacter sp. AU07
Fonte: Braz. j. microbiol;47(3):647-657, July-Sept. 2016. tab, graf.
Idioma: en.
Projeto: Department of Biotechnology, Government of India.
Resumo: ABSTRACT The purpose of this study was to isolate, purify and optimize the production conditions of an organic solvent tolerant and thermostable lipase from Acinetobacter sp. AU07 isolated from distillery waste. The lipase production was optimized by response surface methodology, and a maximum production of 14.5 U/mL was observed at 30 ºC and pH 7, using a 0.5% (v/v) inoculum, 2% (v/v) castor oil (inducer), and agitation 150 rpm. The optimized conditions from the shake flask experiments were validated in a 3 L lab scale bioreactor, and the lipase production increased to 48 U/mL. The enzyme was purified by ammonium sulfate precipitation and ion exchange chromatography and the overall yield was 36%. SDS-PAGE indicated a molecular weight of 45 kDa for the purified protein, and Matrix assisted laser desorption/ionization time of flight analysis of the purified lipase showed sequence similarity with GDSL family of lipases. The optimum temperature and pH for activity of the enzyme was found to be 50 ºC and 8.0, respectively. The lipase was completely inhibited by phenylmethylsulfonyl fluoride but minimal inhibition was observed when incubated with ethylenediaminetetraacetic acid and dithiothreitol. The enzyme was stable in the presence of non-polar hydrophobic solvents. Detergents like SDS inhibited enzyme activity; however, there was minimal loss of enzyme activity when incubated with hydrogen peroxide, Tween 80 and Triton X-100. The kinetic constants (Km and Vmax) revealed that the hydrolytic activity of the lipase was specific to moderate chain fatty acid esters. The Vmax, Km and Vmax/Km ratio of the enzyme were 16.98 U/mg, 0.51 mM, and 33.29, respectively when 4-nitrophenyl palmitate was used as a substrate.
Descritores: Compostos Orgânicos
Solventes
Proteínas de Bactérias/isolamento & purificação
Proteínas de Bactérias/biossíntese
Acinetobacter/enzimologia
Lipase/isolamento & purificação
Lipase/biossíntese
-Compostos Orgânicos/química
Solventes/química
Especificidade por Substrato
Temperatura
Proteínas de Bactérias/química
Estabilidade Enzimática
Cinética
Cromatografia por Troca Iônica
Ativação Enzimática
Espaço Extracelular/enzimologia
Concentração de Íons de Hidrogênio
Íons
Lipase/química
Lipólise
Metais
Peso Molecular
Responsável: BR1.1 - BIREME


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Id: biblio-837660
Autor: Zhang, Wei; Liu, Kang; Li, Lei; Li, Yingxin; Sui, Xianxian; Rao, Yinzhu; Wu, Jiahao; Wu, Qiuping.
Título: Therapeutic effect of low molecular weight chitosan containing sepia ink on ethanol-induced gastric ulcer in rats
Fonte: Acta cir. bras;31(12):813-820, Dec. 2016. graf.
Idioma: en.
Projeto: Spark Program of State Ministry of Science and Technology; . Science and Technology Project of Zhanjiang.
Resumo: ABSTRACT PURPOSE: To evaluate the role of low molecular chitosan containing sepia ink (LMCS) in ethanol-induced (5 ml/kg) gastric ulcer in rats. METHODS: Animals were divided into four groups (n = 12): normal group (Normal), negative control group (Con), experiment group (LMCS) and positive control Omeprazole group (OMZ). Gastric empty rate was detected in the first 7 days. Rats were sacrificed at 7, 14 and 21 day for histology and ELISA detections. RESULTS: Gastric empty was no significant differences among the groups (P > 0.05). Histological observation showed gastric mucosal LMCS treated had better healing effect. Hydroxyproline (Hyp) was significantly increased from 7 day (P < 0.05). LMCS significantly inhibited malondialdehyde (MDA) generation for lipid peroxidation from 7 day (P < 0.05). LMCS significantly promoted the activity of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) at the earlier stage (P < 0.05). OMZ had the similar effects above. As for myeloperoxidase (MPO), LMCS significantly decreased and restored it to normal levels from 7 day (P < 0.05), it is earlier than OMZ which is from 14 day. CONCLUSION: LMCS can improve gastric mucosa tissue repair, exert significant influences on oxidative and antioxidant enzyme activities and neutrophil infiltration.
Descritores: Úlcera Gástrica/tratamento farmacológico
Quitosana/uso terapêutico
Sepia/química
Mucosa Gástrica/efeitos dos fármacos
Antiulcerosos/uso terapêutico
Antioxidantes/farmacologia
-Úlcera Gástrica/induzido quimicamente
Distribuição Aleatória
Quitosana/química
Modelos Animais de Doenças
Etanol
Mucosa Gástrica/patologia
Hidroxiprolina/metabolismo
Tinta
Malondialdeído/metabolismo
Peso Molecular
Antioxidantes/metabolismo
Limites: Animais
Ratos
Responsável: BR1.1 - BIREME


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Id: biblio-1021325
Autor: Al-Soqeer, Abdulrahman A; Alsubaie, Qasi D; Motawei, Mohamed I; Mousa, Hassan M; Abdel-Salam, Ahmed M.
Título: Isolation and identification of allergens and biogenic amines of Prosopis juliflora genotypes
Fonte: Electron. j. biotechnol;30:24-32, nov. 2017. tab, ilus, graf.
Idioma: en.
Resumo: Background: Prosopis, or mesquite (Prosopis juliflora (Sw.) DC.), was introduced in Saudi Arabia several decades ago and is heavily used in street, roadside, and park plantations. It shows great adaptation to the prevailing climatic conditions such as high temperature, severe drought, and salinity and spreads naturally in many parts of the Kingdom. This research was conducted to isolate allergen proteins and biogenic amines from the pollen grains of P. juliflora genotypes in Saudi Arabia from two regions, namely Al-Qassim and Eastern regions. Results: The results showed that 18 different allergen proteins were detected in P. juliflora genotypes, with molecular weight ranging from 14 to 97 kDa. Moreover, P. juliflora genotypes from the two studied regions contained eight biogenic amines, namely histamine, tyramine, tryptamine, ß-phenylethylamine, butricine, codapherine, spermidine, and spermine. All genotypes from the Al-Qassim region were found to contain all eight amines, while in the Eastern region, histamine was absent in three genotypes, spermine was absent in six genotypes, and spermidine was absent in three genotypes. Genotypes B23, E20, and E21 had the lowest biogenic amine quantity. Conclusions: All identified proteins from mesquite trees from both regions (Eastern and Al-Qassim) cause allergies in patients who are sensitive to pollen grains. Bioamines, except histamine and tyramine, were recorded at varying concentrations in different genotypes.
Descritores: Pólen/química
Aminas Biogênicas/isolamento & purificação
Alérgenos/isolamento & purificação
Prosopis
-Proteínas de Plantas/isolamento & purificação
Histamina/isolamento & purificação
Tiramina/isolamento & purificação
Cromatografia Líquida de Alta Pressão
Eletroforese em Gel de Poliacrilamida
Genótipo
Peso Molecular
Responsável: CL1.1 - Biblioteca Central


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Id: biblio-1016095
Autor: Fitriani, Dewi; Rohman, M Saifur; Prijambada, Irfan D.
Título: Proteolytic activity of recombinant DegP from Chromohalobacter salexigens BKL5
Fonte: Electron. j. biotechnol;29:7-12, sept. 2017. ilus, graf, tab.
Idioma: en.
Resumo: Background: DegP is a serine protease that specifically cleaves and refolds unfolding proteins in the periplasmic space of the cells. To date, there is no information regarding DegP from halophilic bacteria. Chromohalobacter salexigens BKL5 is a moderately halophilic bacterium that has the ability to grow in a media containing more than 15% salt. Therefore, the objectives of this work were to clone and overexpress DegP-encoding gene from C. salexigens BKL5 and characterize its biochemical properties. Results: DegP-encoding gene was overexpressed in Escherichia coli BL21(DE3) CodonPlus in an active form. SDS-PAGE analysis showed that the molecular weight of the recombinant DegP was 45 kDa. Size-exclusion chromatography analysis suggested that recombinant DegP was present in two multimeric states, hexameric and dodecameric, with molecular weights of 297.9 and 579.12 kDa, respectively. Both conformations were enzymatically active when casein was used as substrate for enzymatic assay. Circular dichroism analysis showed that recombinant DegP was composed of 0.21­0.29 helical content, which was comparable to the helical content in the crystal structure of E. coli DegP. The basic/acidic residue ratio of recombinant DegP was 0.56, which was slightly higher than that of DegP from extreme halophiles (average, 0.45) but significantly lower than that of DegP from nonhalophiles (average, 0.94). Conclusions: Recombinant DegP from C. salexigens BKL5 showed proteolytic activity when ß-casein was used as a substrate. In silico analysis indicated that recombinant DegP had characteristics similar to those of halophilic proteins depending on its amino acid composition.
Descritores: Serina Endopeptidases/genética
Proteínas Periplásmicas/genética
Chromohalobacter/enzimologia
Proteólise
Proteínas de Choque Térmico/genética
-Proteínas Recombinantes
Serina Endopeptidases/metabolismo
Caseínas
Cromatografia em Gel
Dicroísmo Circular
Clonagem Molecular
Proteínas Periplásmicas/metabolismo
Eletroforese em Gel de Poliacrilamida
Escherichia coli
Salinidade
Chromohalobacter/genética
Proteínas de Choque Térmico/metabolismo
Peso Molecular
Responsável: CL1.1 - Biblioteca Central


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Id: lil-719507
Autor: Antitupa, Isidro; Quispe, William; Mayo, Jhon; Valverde, Fanny; Sanchez, Elizabeth.
Título: Purificación de la fracción antigénica 27-28 KDa a partir del antígeno metabólico secretado-excretado de Fasciola hepatica / Purification of antigenic fraction 27-28 KDa from the metabolic antigen from metabolic secreted-excreted from Fasciola hepatica
Fonte: Rev. peru. med. exp. salud publica;31(2):288-291, abr.-jun. 2014. ilus.
Idioma: es.
Resumo: En el presente estudio, las fracciones antigénicas de 27-28 KDa de Fasciola hepatica fueron purificadas por cromatografía de exclusión molecular para su aplicación en el diagnóstico de la fascioliasis humana. Se obtuvieron antígenos de excreción y secreción a partir de fasciolas adultas vivas obtenida de hígado de ovino y bovino, y cultivados en medio mínimo esencial. La reactividad y eficacia del antígeno purificado fueron evaluadas por la prueba de inmunoblot empleando cuatro sueros con fascioliasis humana; cuatro sueros con otras parasitosis, y dos sueros negativos. Se concluye que las fracciones antigénicas purificadas no presentan reacción cruzada con otras parasitosis, por inmunoblot, por lo que se considera a las proteínas purificadas como potenciales candidatas a ser utilizadas para el diagnóstico de fascioliasis humana.

Antigenic fractions of 27-28 kDa from Fasciola hepatica were purified by size-exclusion chromatography for use in the diagnosis of human fasciolosis. Excretion and secretion antigens were obtained from living adult flukes collected from sheep and cattle liver, and cultured in minimum essential medium. The reactivity of the purified antigen and efficacy were assessed by immunoblot test using four sera with human fascioliasis; four sera with other parasites, and two negative sera. We conclude that the purified antigenic fractions do not cross-react with other parasites by immunoblot. Therefore, purified proteins are considered as potential candidates to be used for the diagnosis of human fascioliasis.
Descritores: Antígenos de Helmintos/isolamento & purificação
Fasciola hepatica/imunologia
-Antígenos de Helmintos/metabolismo
Fasciola hepatica/metabolismo
Fasciolíase/diagnóstico
Peso Molecular
Limites: Humanos
Animais
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME


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Id: biblio-994930
Autor: Vasquez Mejia, Sandra Milena; De Francisco, Alicia; Manique Barreto, Pedro Luiz; Mattioni, Bruna; Zibetti, André Wüst; Molognoni, Luciano; Daguer, Heitor.
Título: Physicochemical comparison of commercial VS. extracted ß-glucans and structural characterization after enzymatic purification / Comparación fisicoquímica entre ß-glucanos comerciales y extraídos, y caracterización estructural después de purificación enzimática
Fonte: Vitae (Medellín);25(1):26-36, 2018. Ilustraciones.
Idioma: en.
Resumo: Background: ß-glucans (1-3: 1-4) are soluble fibers applied to foods due to their technological properties (water binding capacity, viscosity, emulsification and stabilization) and their beneficial effects on health. The functional properties of ß-glucans can be lost during the extraction and purification processes. The high viscosity of ß-glucans is related to a high molecular weight and its physiological properties in the intestine. Therefore, to characterize the fiber after its extraction and purification is fundamental to understand its possible applications in foods. Objectives: characterize ß-glucans extracted (EßG) and compare them with three commercial ß-glucans (CßG-A, CßG-B and CßG-C) to identify its possible applications in foods and to evaluate if enzymatic purification affects molecular and structurally the ß-glucans. Methods: barley ß-glucans were extracted (EßG), characterized by chemical analyzes, rheological behavior, and color, and compared to three commercial ß-glucans samples. Then, the extract was purified and its structural and molecular characteristics were calculated. Results: EßG contained 64.38 ± 3.54% of ß-glucans, high starch contamination (12.70 ± 1.73%), high content of calcium (8894 mg/kg), pseudoplastic behavior, and dark color (L* = 52.77 ± 0.7). All commercial samples showed low starch contamination, lighter color, and Newtonian behavior. After purification starch and protein contamination decreased (0.85 ± 0.46% and 5.50 ± 0.12% respectively), increased the content of ßG (69.45 ± 0.81%) and increased brightness (L* = 92.60 ± 1.70). Purified ß-glucans (PßG) showed a molar weight of 690 ± 1.6 kDa and species with degree polymerization 3 (DP3) to 11 (DP11) were identified on the structure. Conclusions: EßG extracts before the purification presented a high viscosity and contamination. The enzymatic purification process was effective and allowed to maintain a high molar mass of PßG and its distinctive molecular structures (species with DP3 and DP4). The commercial samples CßG-A and CßG-B showed a low content of ß-glucans. Finally, CßG-C presented the best physicochemical and rheological properties for its subsequent application in food.

Antecedentes: los ß-glucanos (1-3: 1-4) son fibras solubles aplicadas a los alimentos debido a sus propiedades tecnológicas (capacidad de retención de agua, viscosidad, emulsificación y estabilización) y a sus efectos beneficiosos en la salud. Las propiedades funcionales de los ß-glucanos pueden perderse durante los procesos de extracción y purificación. La alta viscosidad de los ß-glucanos está relacionada con un alto peso molecular y con sus propiedades fisiológicas en el intestino. Por lo tanto, caracterizar la fibra después de su extracción y purificación es fundamental para comprender sus posibles aplicaciones en alimentos. Objetivos: caracterizar ß-glucanos extraídos (EßG) y compararlos con tres marcas comerciales (CßG-A, CßG-B y CßG-C) para identificar su futura aplicación en alimentos y evaluar si la purificación enzimática afecta molecular y estructuralmente los ß-glucanos. Métodos: se extrajeron ß-glucanos de cebada (EßG), caracterizados por análisis químicos, comportamiento reológico y color, y se compararon con tres muestras comerciales. Posteriormente, el extracto (EßG) se purificó y se identificaron sus características estructurales y su peso molecular. Resultados: EßG contenía 64.38 ± 3.54% de ß-glucanos, alta contaminación con almidón (12.70 ± 1.73%), alto contenido de calcio (8894 mg / kg), comportamiento pseudoplástico y color oscuro (L* = 52.77 ± 0.7). Todas las muestras comerciales mostraron una baja contaminación con almidón, color más claro y comportamiento newtoniano. Después de la purificación de EßG, la contaminación con almidón y proteína disminuyó (0.85 ± 0.46% y 5.50 ± 0.12%, respectivamente), aumentó el contenido de ßG (69.45 ± 0.81%) y aumentó su luminosidad (L* = 92.60 ± 1.70). Los ß-glucanos purificados (PßG) mostraron un peso molar de 690 ± 1,6 kDa y se identificaron en la estructura especies con grado de polimerización desde 3 (GP3) hasta 11 (GP11). Conclusiones: los EßG antes de la purificación presentaron alta viscosidad y contaminación. El proceso de purificación enzimática fue efectivo y permitió mantener una alta masa molar de la fibra y sus estructuras moleculares características (especies con GP3 y GP4). Las muestras comerciales CßG-A y CßG-B mostraron un bajo contenido de ß-glucanos. Finalmente, la CßG-C presentó las mejores propiedades fisicoquímicas y reológicas para su posterior aplicación en alimentos.
Descritores: beta-Glucanas
-Viscosidade
Fibras na Dieta
Alimentos Integrais
Peso Molecular
Limites: Humanos
Tipo de Publ: Artigo Clássico
Responsável: CO56.3 - Biblioteca


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Id: biblio-889234
Autor: Toufiq, Nida; Tabassum, Bushra; Bhatti, Muhammad Umar; Khan, Anwar; Tariq, Muhammad; Shahid, Naila; Nasir, Idrees Ahmad; Husnain, Tayyab.
Título: Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host
Fonte: Braz. j. microbiol;49(2):414-421, Apr.-June 2018. tab, graf.
Idioma: en.
Resumo: Abstract Agricultural crops suffer many diseases, including fungal and bacterial infections, causing significant yield losses. The identification and characterisation of pathogenesis-related protein genes, such as chitinases, can lead to reduction in pathogen growth, thereby increasing tolerance against fungal pathogens. In the present study, the chitinase I gene was isolated from the genomic DNA of Barley (Hordeum vulgare L.) cultivar, Haider-93. The isolated DNA was used as template for the amplification of the ∼935 bp full-length chitinase I gene. Based on the sequence of the amplified gene fragment, class I barley chitinase shares 93% amino acid sequence homology with class II wheat chitinase. Interestingly, barley class I chitinase and class II chitinase do not share sequence homology. Furthermore, the amplified fragment was expressed in Escherichia coli Rosetta strain under the control of T7 promoter in pET 30a vector. Recombinant chitinase protein of 35 kDa exhibited highest expression at 0.5 mM concentration of IPTG. Expressed recombinant protein of 35 kDa was purified to homogeneity with affinity chromatography. Following purification, a Western blot assay for recombinant chitinase protein measuring 35 kDa was developed with His-tag specific antibodies. The purified recombinant chitinase protein was demonstrated to inhibit significantly the important phytopathogenic fungi Alternaria solani, Fusarium spp, Rhizoctonia solani and Verticillium dahliae compared to the control at concentrations of 80 µg and 200 µg.
Descritores: Antifúngicos/farmacologia
Quitinases/farmacologia
Hordeum/enzimologia
Proteínas Recombinantes/metabolismo
-Antifúngicos/química
Antifúngicos/isolamento & purificação
Western Blotting
Quitinases/química
Quitinases/genética
Quitinases/isolamento & purificação
Cromatografia de Afinidade
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Hordeum/genética
Peso Molecular
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Homologia de Sequência de Aminoácidos
Responsável: BR1.1 - BIREME


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Id: biblio-872583
Autor: Fernandes, Liana Bastos Freitas; Rundegren, Jan; Arnebrant, Thomas; Glantz, Per-Olaf.
Título: Characterization of the binding of delmopinol to salivary precipitates / Caracterização da associação de delmopinol com precipitados salivares
Fonte: Braz. dent. j;12(3):173-177, set.-dez. 2001. ilus.
Idioma: en.
Resumo: O objetivo do trabalho é determinar a quantidade de delmopinol associado com cada componente salivar de diferente peso molecular. Saliva não estimulada foi coletada com cinco indivíduos e misturada com delmopinol radioativo obtendo-se uma concentração final de 9,7 mM. As misturas de saliva e delmopinol foram analisadas com eletroforese tanto para o pelete como para o supernatante. Cada amostra foi analisada três vezes em eletroforese. A primeira foi corada com corante de prata. A segunda amostra foi preparada para fazer uma auto-radiografia. A terceira fileira foi cortada em pedaços iguais dissolvidos e analisados com cintilografia. O resultado de cintilografia demonstrou que um grande nível de radioatividade foi detectado em alto peso molecular (600-700 kDa). Em todas as amostras dos peletes foram encontradas grandes quantidades de delmopinol. O resultado da auto-radiografia confirmou que o delmopinol interagiu com proteínas de alto peso molecular (600-700 kDa)
Descritores: Depósitos Dentários/metabolismo
Morfolinas
Proteínas e Peptídeos Salivares/metabolismo
-Autorradiografia
Eletroforese em Gel de Poliacrilamida
Peso Molecular
Ligação Proteica
Saliva
Contagem de Cintilação
Limites: Humanos
Adulto
Pessoa de Meia-Idade
Responsável: BR1.1 - BIREME


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Id: lil-775118
Autor: Sethi, Bijay Kumar; Nanda, Prativa Kumari; Sahoo, Santilata.
Título: Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10
Fonte: Braz. j. microbiol;47(1):143-149, Jan.-Mar. 2016. tab, graf.
Idioma: en.
Projeto: UGC-RGNF Scheme.
Resumo: Abstract Enzyme production by Aspergillus terreus NCFT 4269.10 was studied under liquid static surface and solid-state fermentation using mustard oil cake as a substrate. The maximum lipase biosynthesis was observed after incubation at 30 °C for 96 h. Among the domestic oils tested, the maximum lipase biosynthesis was achieved using palm oil. The crude lipase was purified 2.56-fold to electrophoretic homogeneity, with a yield of 8.44%, and the protein had a molecular weight of 46.3 kDa as determined by SDS-PAGE. Enzyme characterization confirmed that the purified lipase was most active at pH 6.0, temperature of 50 °C, and substrate concentration of 1.5%. The enzyme was thermostable at 60 °C for 1 h, and the optimum enzyme–substrate reaction time was 30 min. Sodium dodecyl sulfate and commercial detergents did not significantly affect lipase activity during 30-min incubation at 30 °C. Among the metal ions tested, the maximum lipase activity was attained in the presence of Zn2+, followed by Mg2+ and Fe2+. Lipase activity was not significantly affected in the presence of ethylenediaminetetraacetic acid, sodium lauryl sulfate and Triton X-100. Phenylmethylsulfonyl fluoride (1 mM) and the reducing, β-mercaptoethanol significantly inhibited lipase activity. The remarkable stability in the presence of detergents, additives, inhibitors and metal ions makes this lipase unique and a potential candidate for significant biotechnological exploitation.
Descritores: Aspergillus/enzimologia
Lipase/metabolismo
-Cátions Bivalentes/metabolismo
Eletroforese em Gel de Poliacrilamida
Estabilidade Enzimática
Ativadores de Enzimas/análise
Inibidores Enzimáticos/análise
Concentração de Íons de Hidrogênio
Lipase/química
Lipase/isolamento & purificação
Peso Molecular
Mercaptoetanol/metabolismo
Metais/metabolismo
Temperatura
Responsável: BR1.1 - BIREME



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