Drucker CT

References (2)

Title : The structure of a Lactobacillus helveticus chlorogenic acid esterase and the dynamics of its insertion domain provide insights into substrate binding - Omori_2023_FEBS.Lett__
Author(s) : Omori KK , Drucker CT , Okumura TLS , Carl NB , Dinn BT , Ly D , Sacapano KN , Tajii A , Owens CP
Ref : FEBS Letters , : , 2023
Abstract : Chlorogenic acid esterases (ChlEs) are a useful class of enzymes that hydrolyze chlorogenic acid (CGA) into caffeic and quinic acid. 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, Gln(145) and Lys(164) , are important for CGA binding. Lys(164) provides a slight substrate preference for CGA, whereas Gln(145) is required for efficient turnover. This work is the first to examine the dynamics of a bacterial ChlE and provides insights on the substrate binding preference and turnover in this type of enzyme.
ESTHER : Omori_2023_FEBS.Lett__
PubMedSearch : Omori_2023_FEBS.Lett__
PubMedID: 37698360
Gene_locus related to this paper: lache-u6f2k7

Title : A highly active esterase from Lactobacillus helveticus hydrolyzes chlorogenic acid in sunflower meal to prevent chlorogenic acid induced greening in sunflower protein isolates - Lo Verde_2022_Food.Res.Int_162_111996
Author(s) : Lo Verde C , Pepra-Ameyaw NB , Drucker CT , Okumura TLS , Lyon KA , Muniz JC , Sermet CS , Were Senger L , Owens CP
Ref : Food Res Int , 162 :111996 , 2022
Abstract : Chlorogenic acid (CGA) is an ester between caffeic and quinic acid. It is found in many foods and reacts with free amino groups in proteins at alkaline pH, leading to the formation of an undesirable green pigment in sunflower seed-derived ingredients. This paper presents the biochemical characterization and application of a highly active chlorogenic acid esterase from Lactobacillus helveticus. The enzyme is one of the most active CGA esterases known to date with a K(m) of 0.090smM and a k(cat) of 82.1ss(-1). The CGA esterase is easily expressed recombinantly in E. coli in large yields and is stable over a wide range of pH and temperatures. We characterized CGA esterase's kinetic properties in sunflower meal and demonstrated that the enzyme completely hydrolyzes CGA in the meal. Finally, we showed that CGA esterase treatment of sunflower seed meal enables the production of pale brown sunflower protein isolates using alkaline extraction. This work will allow for more widespread use of sunflower-derived products in applications where neutrally-colored food products are desired.
ESTHER : Lo Verde_2022_Food.Res.Int_162_111996
PubMedSearch : Lo Verde_2022_Food.Res.Int_162_111996
PubMedID: 36461298
Gene_locus related to this paper: lache-u6f2k7