Document Type
Article
Publication Date
10-12-2022
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 Km of 0.090 mM and a kcat 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.
Recommended Citation
Verde, C. L., Pepra-Ameyaw, N. B., Drucker, C. T., Okumura, T. L. S., Lyon, K. A., Muniz, J. C., Sermet, C. S., Were Senger, L., & Owens, C. P. (2022). A Highly Active Esterase from Lactobacillus helveticus Hydrolyzes Chlorogenic Acid in Sunflower Meal to Prevent Chlorogenic Acid Induced Greening in Sunflower Protein Isolates. Food Research International, 162(A), 111996. https://doi.org/10.1016/j.foodres.2022.111996
Supplementary data 1.
Peer Reviewed
1
Copyright
The authors
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Comments
This article was originally published in Food Research International, volume 162, part A, in 2022. https://doi.org/10.1016/j.foodres.2022.111996