Journal
WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
Volume 32, Issue 1, Pages -Publisher
SPRINGER
DOI: 10.1007/s11274-015-1957-4
Keywords
Endoglucanase; Xylanase; Metagenome; Goat rumen
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Funding
- Education Department Natural Science Foundation of Anhui Province [KJ2013A115]
- Natural Science Foundation of Anhui Province [090411019]
- Specialized Research Fund for the Doctoral Program of Higher Education [20133418120002]
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A cellulase gene (cel28a) was isolated from a rumen microbial metagenome library of goat rumen microorganisms, cloned into E. coli, and expressed in active form. The gene has a length of 1596 bp obtained using a genome walking Kit and encodes a protein of 509 amino acids with a calculated MW of 55 kDa. The deduced amino acid sequence was homologous with cellulases belonging to the glycosyl hydrolase family 5 (GH5). The expressed protein showed activity toward carboxymethylcellulose (CMC) and xylan, suggesting non-specific endoglucanase activity. The optimal conditions for endoglucanase and xylanase activities were 50 degrees C and pH 5.0. The metal ions (Ca2+, Fe2+, Mn2+ and Co2+) stimulated the cellulase activity of cel28a, while the other metal ions and chemicals (Ni2+, Mg2+, Zn2+, Cu2+, SDS and EDTA) inhibited the cellulase activity. Further examination of substrate preference showed a higher activity with CMC, oat spelt xylan and birchwood xylan than with filter paper and microcrystalline cellulose, again suggesting that the protein was an endoglucanase with xylanase activity.
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