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Biochemical characteristics and gene cloning of a novel thermostable feruloyl esterase from Chaetomium sp.
- Yang, Shao-Qing, Tang, Luo, Yan, Qiao-Juan, Zhou, Peng, Xu, Hai-Bo, Jiang, Zheng-Qiang, Zhang, Pan
- Journal of Molecular Catalysis. B, Enzymatic 2013 v.97 pp. 328-336
- Chaetomium, Magnaporthe oryzae, amino acid sequences, amino acids, catalytic activity, feruloyl esterase, gel chromatography, genes, molecular cloning, molecular weight, open reading frames, pH, polyacrylamide gel electrophoresis, substrate specificity, temperature, thermal stability
- A feruloyl esterase from Chaetomium sp. CQ31 was purified and biochemically characterized. The purified feruloyl esterase had a specific activity of 38.6U/mg. The molecular mass of the enzyme was estimated to be 30.2kDa by SDS-PAGE, and 29.6kDa by gel filtration, indicating that the enzyme was a monomer. The optimum pH and temperature of the enzyme were pH 7.5 and 60°C, respectively. It was stable over a broad pH range of 4.0–10.0, and also exhibited good thermostability. The enzyme displayed strict substrate specificity. The Km and Vmax values for methyl ferulate were 0.98μmol/min/mg and 42.6U/mg, respectively. Furthermore, the feruloyl esterase gene was cloned and sequenced. Open reading frame (ORF) of the feruloyl esterase gene (879-bp) encodes 274 amino acids. The deduced amino acid sequence of the feruloyl esterase gene exhibited the highest identity (79%) with that of type B feruloyl esterase from Magnaporthe oryzae.