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Properties and secondary structure of tannase from Penicillium herquei

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Abstract

A tannase with a molecular mass of 72 kDa was obtained from Penicillium herquei isolated from valonia acorns following fermentation in a 5 L bioreactor. This tannase showed optimum activity at pH 6.0 and 30°C. The enzyme was inhibited by Fe3+, Zn2+, dithiothrietol (DTT), β-mercaptoethanol, formaldehyde, and ethanol, and induced by K+, Mn2+, Tween 80, and Triton X-100. The Michaelis constant (K m) and the second-order constant (k cat/K m) values of the tannase for propyl gallate (PG) were 0.62 mM and 174.1 mM/sec. The circular dichroism (CD) spectra indicated that the secondary structure of the tannase contained 14% α helix, 32.4% anti-parallel β-sheet, 4.8% β-sheet, 18.8% β-turn, and 30% random coil. Native tannase in ultrapure water manifested as spherical nano-particle aggregates with diameters ranging from 50 to 300 nm determined by atomic force microscopy (AFM).

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Authors and Affiliations

  1. Laboratory of Ethnopharmacology, Regenerative Medicine Research Center, Institute for Nanobiomedical Technology and Membrane Biology, West China Hospital/West China Medical School, Sichuan University, Chengdu, 610-041, China

    Yu Qiu, Wen Huang, Yang He & Xiao-Hua Wu

  2. Mathematical College, Sichuan University, Chengdu, 610-065, China

    Hai Niu

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  1. Yu Qiu
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  2. Hai Niu
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  3. Wen Huang
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  4. Yang He
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  5. Xiao-Hua Wu
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Correspondence to Wen Huang, Yang He or Xiao-Hua Wu.

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Two authors contributed equally to this work.

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Qiu, Y., Niu, H., Huang, W. et al. Properties and secondary structure of tannase from Penicillium herquei . Biotechnol Bioproc E 16, 858–866 (2011). https://doi.org/10.1007/s12257-011-0123-6

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  • DOI: https://doi.org/10.1007/s12257-011-0123-6

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