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http://dx.doi.org/10.5483/BMBRep.2011.44.1.52

Molecular cloning, expression and characterization of a novel feruloyl esterase enzyme from the symbionts of termite (Coptotermes formosanus) gut  

Chandrasekharaiah, Matam (Rumen Microbiology Laboratory, Animal Nutrition Division, National Institute of Animal Nutrition and Physiology)
Thulasi, Appoothy (Rumen Microbiology Laboratory, Animal Nutrition Division, National Institute of Animal Nutrition and Physiology)
Bagath, M. (Rumen Microbiology Laboratory, Animal Nutrition Division, National Institute of Animal Nutrition and Physiology)
Kumar, Duvvuri Prasanna (Rumen Microbiology Laboratory, Animal Nutrition Division, National Institute of Animal Nutrition and Physiology)
Santosh, Sunil Singh (Rumen Microbiology Laboratory, Animal Nutrition Division, National Institute of Animal Nutrition and Physiology)
Palanivel, Chenniappan (Rumen Microbiology Laboratory, Animal Nutrition Division, National Institute of Animal Nutrition and Physiology)
Jose, Vazhakkala Lyju (Rumen Microbiology Laboratory, Animal Nutrition Division, National Institute of Animal Nutrition and Physiology)
Sampath, K.T. (Rumen Microbiology Laboratory, Animal Nutrition Division, National Institute of Animal Nutrition and Physiology)
Publication Information
BMB Reports / v.44, no.1, 2011 , pp. 52-57 More about this Journal
Abstract
Termites play an important role in the degradation of dead plant materials and have acquired endogenous and symbiotic cellulose digestion capabilities. The feruloyl esterase enzyme (FAE) gene amplified from the metagenomic DNA of Coptotermes formosanus gut was cloned in the TA cloning vector and subcloned into a pET32a expression vector. The Ft3-7 gene has 84% sequence identity with Clostridium saccharolyticum and shows amino acid sequence identity with predicted xylanase/chitin deacetylase and endo-1,4-beta-xylanase. The sequence analysis reveals that probably Ft3-7 could be a new gene and that its molecular mass was 18.5 kDa. The activity of the recombinant enzyme (Ft3-7) produced in Escherichia coli (E.coli) was 21.4 U with substrate ethyl ferulate and its specific activity was 24.6 U/mg protein. The optimum pH and temperature for enzyme activity were 7.0 and $37^{\circ}C$, respectively. The substrate utilization preferences and sequence similarity of the Ft3-7 place it in the type-D sub-class of FAE.
Keywords
Cloning; Expression; Feruloyl esterase; Metagenome; Termite;
Citations & Related Records

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