Feruloyl Esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>: Structural Insights and Functional Characterization for Application in Ferulic Acid Production
Ferulic acid and related hydroxycinnamic acids, used as antioxidants and preservatives in the food, cosmetic, pharmaceutical and biotechnology industries, are among the most abundant phenolic compounds present in plant biomass. Identification of novel compounds that can produce ferulic acid and hydr...
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MDPI AG
2023-07-01
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author | Sangeun Jeon Jisub Hwang Hackwon Do Ly Thi Huong Luu Le Chang Woo Lee Wanki Yoo Min Ju Lee Seung Chul Shin Kyeong Kyu Kim Han-Woo Kim Jun Hyuck Lee |
author_facet | Sangeun Jeon Jisub Hwang Hackwon Do Ly Thi Huong Luu Le Chang Woo Lee Wanki Yoo Min Ju Lee Seung Chul Shin Kyeong Kyu Kim Han-Woo Kim Jun Hyuck Lee |
author_sort | Sangeun Jeon |
collection | DOAJ |
description | Ferulic acid and related hydroxycinnamic acids, used as antioxidants and preservatives in the food, cosmetic, pharmaceutical and biotechnology industries, are among the most abundant phenolic compounds present in plant biomass. Identification of novel compounds that can produce ferulic acid and hydroxycinnamic acids, that are safe and can be mass-produced, is critical for the sustainability of these industries. In this study, we aimed to obtain and characterize a feruloyl esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>. Our results demonstrated that <i>La</i>Fae reacts with ethyl ferulate and can be used to effectively produce ferulic acid from wheat bran, rice bran and corn stalks. In addition, xylanase supplementation was found to enhance <i>La</i>Fae enzymatic hydrolysis, thereby augmenting ferulic acid production. To further investigate the active site configuration of <i>La</i>Fae, crystal structures of unliganded and ethyl ferulate-bound <i>La</i>Fae were determined at 2.3 and 2.19 Å resolutions, respectively. Structural analysis shows that a Phe34 residue, located at the active site entrance, acts as a gatekeeper residue and controls substrate binding. Mutating this Phe34 to Ala produced an approximately 1.6-fold increase in <i>La</i>Fae activity against <i>p</i>-nitrophenyl butyrate. Our results highlight the considerable application potential of <i>La</i>Fae to produce ferulic acid from plant biomass and agricultural by-products. |
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spelling | doaj.art-93e10987201d4fbabcae836a9066ec152023-11-18T16:49:09ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-07-0124131117010.3390/ijms241311170Feruloyl Esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>: Structural Insights and Functional Characterization for Application in Ferulic Acid ProductionSangeun Jeon0Jisub Hwang1Hackwon Do2Ly Thi Huong Luu Le3Chang Woo Lee4Wanki Yoo5Min Ju Lee6Seung Chul Shin7Kyeong Kyu Kim8Han-Woo Kim9Jun Hyuck Lee10Department of Chemistry, College of Natural Science, Sookmyung Women’s University, Seoul 04310, Republic of KoreaResearch Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 07505, Republic of KoreaResearch Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 07505, Republic of KoreaDepartment of Chemistry, College of Natural Science, Sookmyung Women’s University, Seoul 04310, Republic of KoreaResearch Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 07505, Republic of KoreaDepartment of Chemistry, College of Natural Science, Sookmyung Women’s University, Seoul 04310, Republic of KoreaResearch Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 07505, Republic of KoreaDivision of Life Sciences, Korea Polar Research Institute, Incheon 07505, Republic of KoreaDepartment of Precision Medicine, Graduate School of Basic Medical Science (GSBMS), Sungkyunkwan University School of Medicine, Suwon 16419, Republic of KoreaResearch Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 07505, Republic of KoreaResearch Unit of Cryogenic Novel Material, Korea Polar Research Institute, Incheon 07505, Republic of KoreaFerulic acid and related hydroxycinnamic acids, used as antioxidants and preservatives in the food, cosmetic, pharmaceutical and biotechnology industries, are among the most abundant phenolic compounds present in plant biomass. Identification of novel compounds that can produce ferulic acid and hydroxycinnamic acids, that are safe and can be mass-produced, is critical for the sustainability of these industries. In this study, we aimed to obtain and characterize a feruloyl esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>. Our results demonstrated that <i>La</i>Fae reacts with ethyl ferulate and can be used to effectively produce ferulic acid from wheat bran, rice bran and corn stalks. In addition, xylanase supplementation was found to enhance <i>La</i>Fae enzymatic hydrolysis, thereby augmenting ferulic acid production. To further investigate the active site configuration of <i>La</i>Fae, crystal structures of unliganded and ethyl ferulate-bound <i>La</i>Fae were determined at 2.3 and 2.19 Å resolutions, respectively. Structural analysis shows that a Phe34 residue, located at the active site entrance, acts as a gatekeeper residue and controls substrate binding. Mutating this Phe34 to Ala produced an approximately 1.6-fold increase in <i>La</i>Fae activity against <i>p</i>-nitrophenyl butyrate. Our results highlight the considerable application potential of <i>La</i>Fae to produce ferulic acid from plant biomass and agricultural by-products.https://www.mdpi.com/1422-0067/24/13/11170crystal structure<i>La</i>Faeferulic acidferuloyl esteraseX-ray crystallography |
spellingShingle | Sangeun Jeon Jisub Hwang Hackwon Do Ly Thi Huong Luu Le Chang Woo Lee Wanki Yoo Min Ju Lee Seung Chul Shin Kyeong Kyu Kim Han-Woo Kim Jun Hyuck Lee Feruloyl Esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>: Structural Insights and Functional Characterization for Application in Ferulic Acid Production International Journal of Molecular Sciences crystal structure <i>La</i>Fae ferulic acid feruloyl esterase X-ray crystallography |
title | Feruloyl Esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>: Structural Insights and Functional Characterization for Application in Ferulic Acid Production |
title_full | Feruloyl Esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>: Structural Insights and Functional Characterization for Application in Ferulic Acid Production |
title_fullStr | Feruloyl Esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>: Structural Insights and Functional Characterization for Application in Ferulic Acid Production |
title_full_unstemmed | Feruloyl Esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>: Structural Insights and Functional Characterization for Application in Ferulic Acid Production |
title_short | Feruloyl Esterase (<i>La</i>Fae) from <i>Lactobacillus acidophilus</i>: Structural Insights and Functional Characterization for Application in Ferulic Acid Production |
title_sort | feruloyl esterase i la i fae from i lactobacillus acidophilus i structural insights and functional characterization for application in ferulic acid production |
topic | crystal structure <i>La</i>Fae ferulic acid feruloyl esterase X-ray crystallography |
url | https://www.mdpi.com/1422-0067/24/13/11170 |
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