Identification of Thermophilic Bacterial Strains Producing Thermotolerant Hydrolytic Enzymes from Manure Compost

Ten thermophilic bacterial strains were isolated from manure compost. Phylogenetic analysis based on 16S rRNA genes and biochemical characterization allowed identification of four different species belonging to four genera: Geobacillus thermodenitrificans, Bacillus smithii, Ureibacillus suwonensis a...

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Bibliographic Details
Published in:Indian journal of microbiology 2012-03, Vol.52 (1), p.41-47
Main Authors: Charbonneau, David M, Meddeb-Mouelhi, Fatma, Boissinot, Maurice, Sirois, Marc, Beauregard, Marc
Format: Article
Language:English
Subjects:
alpha -Amylase
Aneurinibacillus thermoaerophilus
Bacillus smithii
Bacillus thermodenitrificans
Biomedical and Life Sciences
chemotaxonomy
Composts
enzyme activity
Enzymes
Genes
Geobacillus
heat tolerance
Industrial applications
Laboratories
Life Sciences
Manure
Manures
Medical Microbiology
Microbiology
Microorganisms
Original
Original Article
Phylogenetics
Phylogeny
Polymerase chain reaction
Proteinase
proteinases
Restriction fragment length polymorphism
ribosomal RNA
rRNA
rRNA 16S
thermal stability
thermophilic bacteria
Ureibacillus
Xylan endo-1,3- beta -xylosidase
xylanases
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Summary:Ten thermophilic bacterial strains were isolated from manure compost. Phylogenetic analysis based on 16S rRNA genes and biochemical characterization allowed identification of four different species belonging to four genera: Geobacillus thermodenitrificans, Bacillus smithii, Ureibacillus suwonensis and Aneurinibacillus thermoaerophilus. PCR-RFLP profiles of the 16S-ITS-23S rRNA region allowed us to distinguish two subgroups among the G. thermodenitrificans isolates. Isolates were screened for thermotolerant hydrolytic activities (60–65°C). Thermotolerant lipolytic activities were detected for G. thermodenitrificans, A. thermoaerophilus and B. smithii. Thermotolerant protease, α-amylase and xylanase activities were also observed in the G. thermodenitrificans group. These species represent a source of potential novel thermostable enzymes for industrial applications.
ISSN:0046-8991
0973-7715
DOI:10.1007/s12088-011-0156-8