Open AccessExpression, purification, crystallization and preliminary X‐ray analysis of tannase from Lactobacillus plantarum
Author(s) -
Wu Mingbo,
Peng Xiaohong,
Wen Hua,
Wang Qin,
Chen Qianming,
McKinstry William J.,
Ren Bin
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113006143
Subject(s) - tannase , crystallization , lactobacillus plantarum , gallic acid , chemistry , hydrolysis , dimer , monomer , resolution (logic) , food science , crystallography , bacteria , lactic acid , organic chemistry , biology , polymer , artificial intelligence , computer science , genetics , antioxidant
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 P 1, with unit‐cell paramters 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.