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Streptomyces
Bagaço de cana
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Citação: Cunha, Carolina Cândida de Queiroz Brito - Caracterização de celulases e xilanases produzidas por Streptomyces sp. cultivado em resíduos lignocelulósicos - 2012 - 99 f. - Dissertação - Programa de Pós-graduação em Biologia (ICB) - Universidade Federal de Goiás - Goiânia, 2012.
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ALCÂNTARA, Guizelle Aparecida de. Caracterização farmacognostica e atividade antimicrobiana da folha e casca do caule da myrciarostratadc.(myrtaceae). 2012. 41 f. Dissertação (Mestrado em Ciências Farmacêuticas) - Universidade Federal de Goiás, Goiânia, 2012. on 2014-09-19T13:12:18Z (GMT) / Submitted by Erika Demachki (erikademachki@gmail.com) on 2014-09-22T18:04:37Z
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Previous issue date: 2012-10-27 / Conselho Nacional de Pesquisa e Desenvolvimento Científico e Tecnológico - CNPq / An actinomycete strain, isolated from cane sugar bagasse (CSB), identified as
Streptomyces sp was selected for its ability to produce cellulases. The production of cellulases
was analyzed by submerged fermentation by cultivation on minimal medium (MM)
containing CSB, wheat bran (WB) or carboxymethylcellulose (CMC) as carbon source, and
yeast extract (YE) as nitrogen source. The results show that WB was the best inducer of
CMCases (2.0 U.mL-1). Aiming to analyze the production of cellulases and xylanases
kinetics, the isolate was inoculated in minimal medium containing 0.5% (w/v) WB and
maintained for 12 days at 45°C under constant agitation of 180 rpm. The highest yield of
Avicelase was observed after 264 h of cultivation (5.646 Uml-1), after 144 h for CMCase
(3.872 Uml-1), after 144 h for FPase (0.0947 Uml-1) and after 288 h for Xylanase (92.40 Uml-
1). Culture supernatants with maximum activity of Avicelase, CMCase, Fpase and Xylanase
were analyzed for optima pH and temperature of the respective enzymes. The highest enzyme
activities were detected at pH 7.0 at 35°C for Avicelase, pH 4.5/75°C for CMCase, pH
5.5/45°Cfor FPase and pH 5.5/70°C for Xylanase. The enzymes retained more than 70% of
the initial activity after 2 h incubation at 50°C. The profile proteins analyzed by zymogram
demonstrated a set of secreted cellulases (37, 21 and 17 kDa) and xylanases (39, 21, 18 and
17 kDa) when grown on FT for 144 h. The saccharification assay with CSB as substrate
showed that the enzyme complex was able to release 19% of glucose and 62.9% of xylose. / Uma linhagem de Actinomiceto, isolada do bagaço de cana-de-açúcar (BCA), identificada
como Streptomyces sp foi selecionada pela sua capacidade de produzir celulases. A produção
de celulases foi analisada por fermentação submersa (FS) pelo cultivo do isolado em meio
mínimo (MM) contendo BCA, farelo de trigo (FT) ou carboximetilcelulose (CMC) como
fonte de carbono, e extrato de levedura (EL) como fonte de nitrogênio. Os resultados
demostraram que o FT foi o melhor indutor da produção de CMCases (2,0 U.mL-1). Com o
objetivo de analisar a cinética de produção de celulases e xilanases pelo isolado, este foi
inoculado em meio mínimo contendo 0,5% (w/v) FT e mantido por 12 dias a 45°C sob
agitação constante de 180 rpm. A maior produção de Avicelase foi observada após 264 h de
cultivo (5,646 UmL-1), de CMCase após 144 h (3,872 UmL-1), de FPase após 144 h (0,0947
UmL-1) e de Xilanase após 288 h (92,40 UmL-1). Os sobrenantes de cultura com atividade
máxima de Avicelase, CMCase, FPase e Xilanase foram analisados quanto ao pH e
temperatura ótimos das respectivas enzimas. Os resultados obtidos demonstraram que a maior
atividade de Avicelase foi detectada em pH 7,0 a 35°C; CMCase apresentou melhor atividade
em pH 4,5 a 75°C; FPase apresentou melhor atividade em pH 5,5 a 45°C e Xilanase
apresentou melhor atividade em pH 5,5 a 70°C. Quanto à termoestabilidade, as enzimas
presentes mantiveram mais de 70% da atividade inicial após 2 h de incubação a 50°C. O perfil
de proteínas analisado por zimograma demonstrou que o isolado secretou um conjunto de
celulases (37, 21 e 17 KDa) e xilanases (39, 21, 18 e 17 KDa) quando cultivado em FT por
144 h. No ensaio de sacarificação de BCA o complexo enzimático foi capaz de liberar 19% de
glicose e 62,9% de xilose.
Identifer | oai:union.ndltd.org:IBICT/oai:repositorio.bc.ufg.br:tede/3119 |
Date | 27 October 2012 |
Creators | Cunha, Carolina Cândida de Queiroz Brito |
Contributors | Bataus, Luiz Artur Mendes |
Publisher | Universidade Federal de Goiás, Programa de Pós-graduação em Biologia (ICB), UFG, Brasil, Instituto de Ciências Biológicas - ICB (RG) |
Source Sets | IBICT Brazilian ETDs |
Language | Portuguese |
Detected Language | Portuguese |
Type | info:eu-repo/semantics/publishedVersion, info:eu-repo/semantics/masterThesis |
Format | application/pdf |
Source | reponame:Biblioteca Digital de Teses e Dissertações da UFG, instname:Universidade Federal de Goiás, instacron:UFG |
Rights | http://creativecommons.org/licenses/by-nc-nd/4.0/, info:eu-repo/semantics/openAccess |
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