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Characterization of a tannin acyl hydrolase from Streptomyces sviceus with substrate preference for digalloyl ester bonds

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Abstract

The search for new tannases with novel enzymatic properties suitable for industrial applications has been a continuous effort since the first discovery of the enzyme more than a century ago. A tannase gene (Ss-Tan) from the Gram-positive bacterium Streptomyces sviceus was identified, chemically synthesized, and cloned into a C-terminal His-tagged vector for expression in Escherichia coli. The tannase possesses the active site motif of GXSXG that is conserved for serine hydrolases. The residues that constitute the catalytic triad and galloyl binding site in bacterial tannases are found conserved in Ss-Tan, which include Ser209, Asp452, His484 and Lys370, Glu384, Asp454, respectively. Ss-Tan was overexpressed in E. coli BL21-AI cells with high productivity. Enzymatic assay revealed that the enzyme displays tannase activities to hydrolyze both the ester bonds and depside bonds in hydrolyzable tannins. Kinetic analysis indicated that the enzyme preferentially acts on depside bonds with considerably higher substrate affinity and catalytic efficiency. The enzyme showed maximum activity around pH 8.0 and at 50 °C with the highest melting temperature close to 70 °C. The high depsidase activity and thermostablility of Ss-Tan may make the enzyme suitable for potential industrial applications to achieve complete digestion of hydrolyzable tannins.

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Acknowledgments

This work was supported by the CSIRO Materials Science and Engineering Bioscience Program and CSIRO Transformational Biology Capability Platform for enhancing recombinant protein production. We thank the Structural Genomics Consortium for the provision of the pNIC-CH cloning vector and Dr. Shane Seabrook for performing DSF. MW visit to CSIRO was supported by the China Scholarship Council (CSC).

Conflict of interest

The authors declare that they have no conflict of interest.

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Authors and Affiliations

  1. Materials Science and Engineering, CSIRO, 343 Royal Parade, Parkville, VIC, 3052, Australia

    Mingbo Wu, William J. McKinstry & Bin Ren

  2. State Key Laboratory of Oral Diseases, West China College of Stomatology, Sichuan University, 610041, Chengdu, China

    Mingbo Wu

  3. Institute of Nanobiomedical Technology and Membrane Biology, State Key Laboratory of Biotherapy, Sichuan University, 610041, Chengdu, China

    Qin Wang

Authors
  1. Mingbo Wu
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  2. Qin Wang
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  3. William J. McKinstry
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  4. Bin Ren
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Corresponding author

Correspondence to Bin Ren.

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Author contributions

BR conceived the project. MW and QW performed the experiments under the supervision of BR and WJM. BR wrote the manuscript.

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Wu, M., Wang, Q., McKinstry, W.J. et al. Characterization of a tannin acyl hydrolase from Streptomyces sviceus with substrate preference for digalloyl ester bonds. Appl Microbiol Biotechnol 99, 2663–2672 (2015). https://doi.org/10.1007/s00253-014-6085-9

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  • DOI: https://doi.org/10.1007/s00253-014-6085-9

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