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

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, ? = 70.4, ? = 86.0, ? = 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.

SUBMITTER: Wu M

PROVIDER: S-EPMC3614178 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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

Wu Mingbo M Peng Xiaohong X Wen Hua H Wang Qin Q Chen Qianming Q McKinstry William J WJ Ren Bin B

Acta crystallographica. Section F, Structural biology and crystallization communications 20130328 Pt 4

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 ...[more]

PMID: 23545659

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