Base de dados : LILACS
Pesquisa : D09.947.875.627.166 [Categoria DeCS]
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Texto completo SciELO Brasil
Texto completo
Id: biblio-1055382
Autor: Laboratory of Biochemical EngineeringFreitas, Bárbara Catarina Bastos de; Laboratory of Biochemical EngineeringCassuriaga, Ana Paula Aguiar; Laboratory of Microbiology and BiochemistryMorais, Michele Greque de; Atala, Daniel Ibraim Pires; Laboratory of Biochemical EngineeringCosta, Jorge Alberto Vieira.
Título: Pentoses Used in Cultures of Synechococcus nidulans and Spirulina paracas: Evaluation of Effects in Growth and in Content of Proteins and Carbohydrates
Fonte: Braz. arch. biol. technol;62:e19180728, 2019. tab, graf.
Idioma: en.
Resumo: Abstract The biological assimilation of the sugars present in lignocellulosic residues has gained prominence since these residues are the most abundant and economic residues in nature. Thus, the objective of this work was to determine whether the use of D-xylose and L-arabinose as sources of carbon in Synechococcus nidulans and Spirulina paracas cultures affects the growth and production of proteins and carbohydrates. Kinetic growth parameters, pentose consumption, protein content and carbohydrates were evaluated. Synechococcus nidulans and Spirulina paracas consumed all concentrations of pentose used. The highest cellular concentration (1.37 g.L-1) and the highest protein productivity (54 mg.L-1.d-1) were obtained for Spirulina paracas, which was submitted to the addition of 38.33 mg.L-1 D-xylose and 1.79 mg.L-1 L-arabinose. The use of pentose promoted the accumulation of proteins for the studied microalgae. This is one of the first works to report protein bioaccumulation as a result of pentose addition.
Descritores: Arabinose/administração & dosagem
Xilose/administração & dosagem
Proteínas/efeitos dos fármacos
Responsável: BR1.1 - BIREME

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Id: biblio-1048179
Autor: Gao, Juan; Zhao, Yan; Zhang, Guocai; Li, Yumei; Li, Qiang.
Título: Production optimization, purification, expression, and characterization of a novel α-L-arabinofuranosidase from Paenibacillus polymyxa
Fonte: Electron. j. biotechnol;36:24-33, nov. 2018. graf, tab, ilus.
Idioma: en.
Projeto: National Natural Science Foundation of China; . Shandong Provincial Natural Science Foundation.
Resumo: Background: α-L-Arabinofuranosidase (EC catalyzes the hydrolysis of terminal α-L-1,2-, -1,3-, and -1,5- arabinofuranosyl residues in arabinose-containing polymers, and hence, it plays an important role in hemicellulose degradation. Herein, the bacterium Paenibacillus polymyxa, which secretes arabinofuranosidase with high activity, was selected for enzyme production, purification, and characterization. Results: Medium components and cultural conditions were optimized by the response surface method using shake flask cultures. Arabinofuranosidase production reached 25.2 U/mL under optimized conditions, which were pH 7.5, 28°C, and a basic medium supplemented with 1.5 g/L mannitol and 3.5 g/L soymeal. Furthermore, the arabinofuranosidase secreted by P. polymyxa, named as PpAFase-1, was partially purified from the supernatant using a DEAE Sepharose Fast Flow column and a hydroxyapatite column. The approximate molecular mass of the purified PpAFase-1 was determined as 56.8 kDa by SDS-PAGE. Protein identification by mass spectrometry analysis showed that the deduced amino acid sequence had significant similarity to the glycosyl hydrolase family 51. The deduced gene of 1515 bp was cloned and expressed in Escherichia coli BL21 (DE3) cells. Purified recombinant PpAFase-1 was active toward p-nitrophenyl-α-L-arabinofuranoside (pNPAraf). The Km and kcat values toward pNPAraf were 0.81 mM and 53.2 s−1 , respectively. When wheat arabinoxylan and oat spelt xylan were used as substrates, PpAFase-1 showed poor efficiency. However, a synergistic effect was observed when PpAFase-1 was combined with xylanase from Thermomyces lanuginosus. Conclusion: A novel GH51 enzyme PpAFase-1 was cloned from the genome of P. polymyxa and expressed in E. coli. This enzyme may be suitable for hemicellulose degradation on an industrial scale.
Descritores: Paenibacillus polymyxa/enzimologia
Glicosídeo Hidrolases/metabolismo
Espectrometria de Massas
Eletroforese em Gel de Poliacrilamida
Glicosídeo Hidrolases/isolamento & purificação
Glicosídeo Hidrolases/biossíntese
Responsável: CL1.1 - Biblioteca Central

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Curi, R
Alvarez, M
Bazotte, Roberto Barbosa
Botion, L. M
Bracht, A
Id: lil-42016
Autor: Curi, R; Alvarez, M; Bazotte, Roberto Barbosa; Botion, L. M; Godoy, J. L; Bracht, A.
Título: Effect of Stevia rebaudiana on glucose tolerance in normal adult humans
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;19(6):771-4, 1986. ilus.
Idioma: en.
Descritores: Arabinose/farmacologia
Teste de Tolerância a Glucose
Extratos Vegetais/farmacologia
Limites: Humanos
Tipo de Publ: Estudo Comparativo
Responsável: BR1.1 - BIREME

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