Biochemical and Structural Characterization of a Novel Bacterial Tannase From Lachnospiraceae bacterium in Ruminant Gastrointestinal Tract

Tannases are a family of esterases that catalyze the hydrolysis of ester and depside bonds present in hydrolyzable tannins to release gallic acid. Here, a novel tannase from Lachnospiraceae bacterium (TanA(Lb)) was characterized. The recombinant TanA(Lb) exhibited maximal activity at pH 7.0 and 50 degrees C, and it maintained more than 70% relative activity from 30 degrees C to 55 degrees C. The activity of TanA(Lb) was enhanced by Mg2+ and Ca2+, and was dramatically reduced by Cu2+ and Mn2+. TanA(Lb) is capable of degrading esters of phenolic acids with long-chain alcohols, such as lauryl gallate as well as tannic acid. The Km value and catalytic efficiency (k(cat) /Km) of TanA(Lb) toward five substrates showed that tannic acid (TA) was the favorite substrate. Homology modeling and structural analysis indicated that TanA(Lb) contains an insertion loop (residues 341-450). Based on the moleculer docking and molecular dynamics (MD) simulation, this loop was observed as a flap-like lid to interact with bulk substrates such as tannic acid. TanA(Lb) is a novel bacterial tannase, and the characteristics of this enzyme make it potentially interesting for industrial use.

Automated summary

TanA(Lb) is a novel bacterial tannase with optimal activity at neutral pH and higher temperatures, regulated by beneficial metal ions. It shows high affinity and catalytic efficiency towards tannic acid, with structural analysis revealing its interaction with substrates.