Use este identificador para citar ou linkar para este item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/981473
Título: Endo- and exoglucanase activities in bacteria from mangrove sediment.
Autoria: SOARES JUNIOR, F. L.
DIAS, A. C. F.
FASANELLA, C. C.
TAKETANI, R. G.
LIMA, A. O. S.
MELO, I. S. de
ANDREOTE, F. D.
Afiliação: FABIO LINO SOARES JUNIOR, ESALQ-USP; ARMANDO CAVALCANTE FRANCO DIAS, CENA-USP; CRISTIANE CIPOLA FASANELLA, ESALQ-USP; RODRIGO GOUVEA TAKETANI; ANDRE OLIVEIRA DE SOUZA LIMA, UNIVALI; ITAMAR SOARES DE MELO, CNPMA; FERNANDO DINI ANDREOTE, ESALQ-USP.
Ano de publicação: 2013
Referência: Brazilian Journal of Microbiology, Piracicaba, v. 44, n. 3, p. 969-976, 2013.
Conteúdo: The mangrove ecosystem is an unexplored source for biotechnological applications. In this unique environment, endemic bacteria have the ability to thrive in the harsh environmental conditions (salinity and anaerobiosis), and act in the degradation of organic matter, promoting nutrient cycles. Thus, this study aimed to assess the cellulolytic activities of bacterial groups present in the sediment from amangrove located in Ilha do Cardoso (SP, Brazil). To optimize the isolation of cellulolytic bacteria,enrichments in two types of culture media (tryptone broth and minimum salt medium), both supplementedwith 5% NaCl and 1% of cellulose, were performed. Tests conducted with the obtained colonies showed a higher occurrence of endoglycolytic activity (33 isolates) than exoglycolytic (19 isolates), and the degradation activity was shown to be modulated by the presence of NaCl. The isolated bacteria were clustered by BOX-PCR and further classified on the basis of partial 16S rRNA sequences as Alphaproteobacteria, Gammaproteobacteria, Actinobacteria, Firmicutes or Bacteroidetes. Therefore, this study highlights the importance of studies focusing on the endemic species found in mangroves to exploit them as novel biotechnological tools for the degradation of cellulose.
NAL Thesaurus: salinity
Palavras-chave: Cellulose, Endo-1,4-B-D-glucanase
Exo-1,4-B-D-glucanase
Tipo do material: Artigo de periódico
Acesso: openAccess
Aparece nas coleções:Artigo em periódico indexado (CNPMA)

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