Novel hydrolase diversity retrieved from a metagenome library of bovine rumen microflora (Articolo in rivista)

Type
Label
  • Novel hydrolase diversity retrieved from a metagenome library of bovine rumen microflora (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • FERRER, M., GOLYSHINA, O.V., CHERNIKOVA, T.N., KHACHANE, K., REYES-DUARTE, D., MARTINS DOS SANTOS, V.A.P., STROMPL, C., ELBOROUGH, K., JARVIS, G., NEEF, A., YAKIMOV, M.M., A.N., TIMMIS, K.N. AND GOLYSHIN, P.N. (2005)
    Novel hydrolase diversity retrieved from a metagenome library of bovine rumen microflora
    in Environmental microbiology (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • FERRER, M., GOLYSHINA, O.V., CHERNIKOVA, T.N., KHACHANE, K., REYES-DUARTE, D., MARTINS DOS SANTOS, V.A.P., STROMPL, C., ELBOROUGH, K., JARVIS, G., NEEF, A., YAKIMOV, M.M., A.N., TIMMIS, K.N. AND GOLYSHIN, P.N. (literal)
Pagina inizio
  • 1996 (literal)
Pagina fine
  • 2012 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 7 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Microbiology, GBF– German Research Centre for Biotechnology, Mascheroder Weg 1, Braunschweig, Germany - Institute of Catalysis, CSIC, Marie Curie 2, Cantoblanco, Madrid, Spain - Institute of Microbiology, Technical University Braunschweig, Germany - ViaLactia Biosciences Limited, Newmarket, Auckland, New Zealand (literal)
Titolo
  • Novel hydrolase diversity retrieved from a metagenome library of bovine rumen microflora (literal)
Abstract
  • A metagenome expression library of bulk DNA extracted from the rumen content of a dairy cow was established in a phage lambda vector and activity-based screening employed to explore the functional diversity of the microbial flora. Twenty-two clones specifying distinct hydrolytic activities (12 esterases, nine endo-²-1,4-glucanases and one cyclodextrinase) were identified in the library and characterized. Sequence analysis of the retrieved enzymes revealed that eight (36%) were entirely new and formed deep-branched phylogenetic lineages with no close relatives among known ester- and glycosyl-hydrolases. Bioinformatic analyses of the hydrolase gene sequences, and the sequences and contexts of neighbouring genes, suggested tentative phylogenetic assignments of the rumen organisms producing the retrieved enzymes. The phylogenetic novelty of the hydrolases suggests that some of them may have potential for new applications in biocatalysis. (literal)
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