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Braz. j. microbiol ; 49(2): 429-442, Apr.-June 2018. tab, graf
Article in English | LILACS | ID: biblio-889226

ABSTRACT

Abstract Bacteria are important sources of cellulases with various industrial and biotechnological applications. In view of this, a non-hemolytic bacterial strain, tolerant to various environmental pollutants (heavy metals and organic solvents), showing high cellulolytic index (7.89) was isolated from cattle shed soil and identified as Bacillus sp. SV1 (99.27% pairwise similarity with Bacillus korlensis). Extracellular cellulases showed the presence of endoglucanase, total cellulase and β-glucosidase activities. Cellulase production was induced in presence of cellulose (3.3 times CMCase, 2.9 times FPase and 2.1 times β-glucosidase), and enhanced (115.1% CMCase) by low-cost corn steep solids. An in silico investigation of endoglucanase (EC 3.2.1.4) protein sequences of three Bacillus spp. as query, revealed their similarities with members of nine bacterial phyla and to Eukaryota (represented by Arthropoda and Nematoda), and also highlighted of a convergent and divergent evolution from other enzymes of different substrate [(1,3)-linked beta-d-glucans, xylan and chitosan] specificities. Characteristic conserved signature indels were observed among members of Actinobacteria (7 aa insert) and Firmicutes (9 aa insert) that served as a potential tool in support of their relatedness in phylogenetic trees.


Subject(s)
Animals , Cattle , Bacillus/enzymology , Cellulase/genetics , Cellulase/metabolism , Evolution, Molecular , Bacillus/growth & development , Bacillus/isolation & purification , Cellulose/metabolism , Computational Biology , Feces/microbiology , Gene Expression Regulation, Bacterial , Gene Expression Regulation, Enzymologic , INDEL Mutation , Sequence Analysis, DNA , Sequence Homology , Substrate Specificity , Zea mays/metabolism
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