The structure of a Lactobacillus helveticus chlorogenic acid esterase and the dynamics of its insertion domain provide insights into substrate binding

Abstract

Chlorogenic acid esterases (ChlEs) are a useful class of enzymes that hydrolyze chlorogenic acid (CGA) into caffeic and quinic acids. ChlEs can break down CGA in foods to improve their sensory properties and release caffeic acid in the digestive system to improve the absorption of bioactive compounds. This work presents the structure, molecular dynamics, and biochemical characterization of a ChlE from Lactobacillus helveticus (Lh). Molecular dynamics simulations suggest that substrate access to the active site of LhChlE is modulated by two hairpin loops above the active site. Docking simulations and mutational analysis suggest that two residues within the loops, Gln145 and Lys164, are important for CGA binding. Lys164 provides a slight substrate preference for CGA, whereas Gln145 is required for efficient turnover. This work is the first to examine the dynamics of a bacterial ChlE and provides insights on substrate binding preference and turnover in this type of enzyme.

Comparative genomics and fermentation flavor characterization of five selected lactic acid bacteria provide predictions for flavor biosynthesis metabolic pathways in fermented muskmelon puree

“…An interesting finding was that quinic acid was detected in all FMPs, whereas it was not detected in fresh and control samples. A study showed that chlorogenic acid esterase in Lactobacillus helveticus had the ability to split chlorogenic acid into caffeic acid and quinic acid (Omori et al, 2023). Subsequent reduction or oxidation reactions metabolized quinic acid into shikimic acid and 3,4,5-trihydroxycyclohexane-1-carboxylic acid, or protocatechuic acid and catechol (Markkinen et al, 2022).…”