Expression, purification, crystallization and preliminary X-ray analysis of tannase from Lactobacillus plantarum

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):456-9. doi: 10.1107/S1744309113006143. Epub 2013 Mar 28.

Abstract

Tannase catalyses the hydrolysis of the galloyl ester bond of tannins to release gallic acid. It belongs to the serine esterases and has wide applications in the food, feed, beverage, pharmaceutical and chemical industries. The tannase from Lactobacillus plantarum was cloned, expressed and purified. The protein was crystallized by the sitting-drop vapour-diffusion method with microseeding. The crystals belonged to space group P1, with unit-cell parameters a = 46.5, b = 62.8, c = 83.8 Å, α = 70.4, β = 86.0, γ = 79.4°. Although the enzyme exists mainly as a monomer in solution, it forms a dimer in the asymmetric unit of the crystal. The crystals diffracted to beyond 1.60 Å resolution using synchrotron radiation and a complete data set was collected to 1.65 Å resolution.

Keywords: Lactobacillus plantarum; hydrolase; tannase; tannin.

MeSH terms

  • Carboxylic Ester Hydrolases / chemistry*
  • Carboxylic Ester Hydrolases / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression
  • Lactobacillus plantarum / enzymology*

Substances

  • Carboxylic Ester Hydrolases
  • tannase