Kinetic and thermodynamic parameters, and partial characterization of the crude extract of tannase produced by Saccharomyces cerevisiae CCMB 520

Nat Prod Res. 2018 May;32(9):1068-1075. doi: 10.1080/14786419.2017.1380010. Epub 2017 Sep 20.

Abstract

Tannase can be used in different industrial sectors such as in food (juices and wine) and pharmaceutical production (trimethoprim) because it catalyses the hydrolysis of hydrolysable tannins. The aim of the current study is to assess the tannase found in the crude extract of Saccharomyces cerevisiae CCMB 520, and to set its catalytic and thermodynamic properties. The enzyme was optimally active at pH 6.0 and temperature 30 °C. Tannase was activated by Na+, Ca2+, K+ at 5 × 10-3 mol/L. The half-life at 30 °C was 3465.7 min. The activation energy was 40.32 kJ/mol. The Gibbs free energy, enthalpy and entropy at 30 °C were 85.40, 48.10 and -0.12 kJ/mol K, respectively. Our results suggest that the tannase found in the crude extract of S. cerevisiae is an attractive enzyme for industrial applications, such as for beverage manufacturing and gallic acid production, due its catalytic and thermodynamic properties (heat-stable and resistant to metal ions).

Keywords: Catalytic properties; Doehlert design; submerged fermentation; tannin acyl hydrolase; thermodynamics.

MeSH terms

  • Carboxylic Ester Hydrolases / chemistry*
  • Carboxylic Ester Hydrolases / metabolism*
  • Catalysis
  • Enzyme Stability
  • Half-Life
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Kinetics
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism
  • Temperature
  • Thermodynamics

Substances

  • Saccharomyces cerevisiae Proteins
  • Carboxylic Ester Hydrolases
  • tannase