Efficient screening of potential cellulases and hemicellulases produced by Bosea sp. FBZP-16 using the combination of enzyme assays and genome analysis
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články
PubMed
28058637
DOI
10.1007/s11274-016-2198-x
PII: 10.1007/s11274-016-2198-x
Knihovny.cz E-zdroje
- Klíčová slova
- Bosea, Cellulases, Enzyme assays, Genome sequencing, Hemicellulases,
- MeSH
- Actinobacteria genetika izolace a purifikace MeSH
- bakteriální proteiny genetika metabolismus MeSH
- celulasa genetika metabolismus MeSH
- celulosa metabolismus MeSH
- fylogeneze MeSH
- glykosidhydrolasy genetika metabolismus MeSH
- lignin metabolismus MeSH
- Proteobacteria genetika izolace a purifikace MeSH
- půda MeSH
- půdní mikrobiologie MeSH
- Rhizobiaceae enzymologie genetika izolace a purifikace MeSH
- RNA ribozomální 16S genetika MeSH
- sekvenční analýza RNA metody MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- celulasa MeSH
- celulosa MeSH
- glykosidhydrolasy MeSH
- hemicellulase MeSH Prohlížeč
- lignin MeSH
- lignocellulose MeSH Prohlížeč
- půda MeSH
- RNA ribozomální 16S MeSH
Identification of bacteria that produce carbohydrolytic enzymes is extremely important given the increased demand for these enzymes in many industries. Twenty lignocellulose-degrading bacterial isolates from Algerian compost and different soils were screened for their potential to produce different enzymes involved in biomass deconstruction. Based on 16S rRNA gene sequencing, the isolates belonged to Proteobacteria and Actinobacteria. Differences among species were reflected both as the presence/absence of enzymes or at the level of enzyme activity. Among the most active species, Bosea sp. FBZP-16 demonstrated cellulolytic activity on both amorphous cellulose (CMC) and complex lignocellulose (wheat straw) and was selected for whole-genomic sequencing. The genome sequencing revealed the presence of a complex enzymatic machinery required for organic matter decomposition. Analysis of the enzyme-encoding genes indicated that multiple genes for endoglucanase, xylanase, β-glucosidase and β-mannosidase are present in the genome with enzyme activities displayed by the bacterium, while other enzymes, such as certain cellobiohydrolases, were not detected at the genomic level. This indicates that a combination of functional screening of bacterial cultures with the use of genome-derived information is important for the prediction of potential enzyme production. These results provide insight into their possible exploitation for the production of fuels and chemicals derived from plant biomass.
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Syst Appl Microbiol. 2014 Feb;37(1):60-7 PubMed
J Biotechnol. 2006 Sep 1;125(2):198-209 PubMed
Mol Biol Evol. 1987 Jul;4(4):406-25 PubMed
Sci Rep. 2015 Feb 10;5:8365 PubMed
Nature. 1964 May 30;202:928-9 PubMed
Nucleic Acids Res. 2012 Jul;40(Web Server issue):W445-51 PubMed
J Gen Microbiol. 1965 Feb;38:251-61 PubMed
Nucleic Acids Res. 2014 Jan;42(Database issue):D206-14 PubMed
Biotechnol Biofuels. 2014 Dec 13;7(1):175 PubMed
Enzyme Res. 2012;2012:793708 PubMed
Mol Biol Evol. 2013 Dec;30(12):2725-9 PubMed
Appl Microbiol Biotechnol. 2014 Feb;98(4):1531-7 PubMed
ISME J. 2011 Aug;5(8):1323-31 PubMed
J Chem Technol Biotechnol. 2015 Mar;90(3):573-581 PubMed
Braz J Microbiol. 2014 Aug 29;45(2):743-56 PubMed
Int J Syst Evol Microbiol. 2014 Feb;64(Pt 2):352-6 PubMed
BMC Genomics. 2008 Feb 08;9:75 PubMed
Sci Rep. 2016 Apr 29;6:25279 PubMed
Microbiology. 2006 Dec;152(Pt 12):3613-22 PubMed
PLoS One. 2014 Dec 02;9(12):e114138 PubMed
Int J Biol Sci. 2009 Jul 29;5(5):500-16 PubMed
J Mol Evol. 1980 Dec;16(2):111-20 PubMed
Enzyme Microb Technol. 2015 Sep;77:38-45 PubMed
Biotechnol Biofuels. 2013 Aug 10;6(1):115 PubMed
PLoS One. 2014 Feb 13;9(2):e89108 PubMed
Front Bioeng Biotechnol. 2015 Jun 16;3:84 PubMed
FEMS Microbiol Rev. 2008 May;32(3):501-21 PubMed
Proc Natl Acad Sci U S A. 2004 Jul 27;101(30):11030-5 PubMed
Enzyme Microb Technol. 2014 Jan 10;54:1-7 PubMed