Biochemical characterization of a novel thermostable feruloyl esterase from Geobacillus thermoglucosidasius DSM 2542.

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ID: 57132
2019
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Abstract
The ferulic acid esterase (FAE) gene from Geobacillus thermoglucosidasius DSM 2542 was cloned into pET28a(+) expression vector and characterized and is being reported in this study for the first time in Geobacillus. The enzyme, designated as GthFAE, was purified by heat shock and ion-exchange column chromatography. In addition, a second clone containing a Histidine tag was expressed and purified by affinity column chromatography demonstrating future potential for scale-up. FAE gene contains an open reading frame (ORF) of 759-bp encoding a hypothetical 252 amino acid protein, a molecular mass of 28.11 kDa and an isoelectric point of 5.53. From this study it was found that GthFAE had optimal activity at 50 °C and pH of 8.5. Furthermore, the enzyme has been found to retain 64% of its activity after two days incubation at 50 °C and exhibited a high level of functionality with p-nitrophenyl caprylate (C8). K, V, k and k/K values for p-nitrophenyl caprylate were determined as 0.035 mM, 11,735 µmol/min/mg protein, 5491 (1/s) and 156,885 s mM respectively. The combination of higher activity and stability compared to previously reported FAEs makes GthFAE a potential candidate for use in the paper manufacturing industry.
Reference Key
ay-sal2019biochemicalmolecular Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Ay Sal, Fulya;Colak, Dilsat Nigar;Guler, Halil Ibrahim;Canakci, Sabriye;Belduz, Ali Osman;
Journal molecular biology reports
Year 2019
DOI
10.1007/s11033-019-04893-6
URL
Keywords
feruloyl esterase geobacillus recombinant thermostable

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