A highly active esterase from Lactobacillus helveticus hydrolyzes chlorogenic acid in sunflower meal to prevent chlorogenic acid induced greening in sunflower protein isolates. (December 2022)

• Record Type: Journal Article
• Authors: Lo Verde, Christine; Pepra-Ameyaw, Nana Baah; Drucker, Charles T.; Okumura, Tracie L.S.; Lyon, Katherine A.; Muniz, Julia C.; Sermet, Chloe S.; Were Senger, Lilian; Owens, Cedric P.
• Is Part Of: Food research international. Volume 162(2022)Part A
• Publication Date: 2022-12
• Subjects: Chlorogenic acid esterase -- Hydrolase kinetics -- Lactobacillus helveticus -- Sunflower protein -- Sunflower seeds; CA caffeic acid -- CD circular dichroism -- CGA Chlorogenic acid -- DLS dynamic light scattering -- HEPES 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid -- HPLC high performance liquid chromatography -- IPTG Isopropyl β-d-1-thiogalactopyranoside -- MALDI-TOF matrix-assisted laser desorption/ionization – time of flight -- QA quinic acid -- SDS-PAGE sodium dodecyl sulfate–polyacrylamide gel electrophoresis -- SFM sunflower meal -- SPI sunflower protein isolate; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2022.111996
• Languages: English
• ISSNs: 0963-9969

Abstract

Graphical abstract: Highlights: L. helveticus chlorogenic acid (CGA) esterase was effective at hydrolyzing CGA. CGA esterase was thermostable, easily expressed, and purified. CGA esterase hydrolyzed CGA in solution and in suspended sunflower seed meal. CGA esterase hydrolyzed CGA in undefatted and defatted sunflower seed meal. CGA hydrolysis fully eliminates CGA-induced greening in sunflower protein isolates. 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 0.090 mM and a k cat of 82.1 s −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.