Feruloyl Esterase (LaFae) from Lactobacillus acidophilus: Structural Insights and Functional Characterization for Application in Ferulic Acid Production

被引:5
作者
Jeon, Sangeun [1 ]
Hwang, Jisub [2 ,3 ]
Do, Hackwon [2 ,3 ]
Le, Ly Thi Huong Luu [1 ]
Lee, Chang Woo [2 ]
Yoo, Wanki [1 ,4 ]
Lee, Min Ju [2 ]
Shin, Seung Chul [5 ]
Kim, Kyeong Kyu [4 ]
Kim, Han-Woo [2 ,3 ]
Lee, Jun Hyuck [2 ,3 ]
机构
[1] Sookmyung Womens Univ, Coll Nat Sci, Dept Chem, Seoul 04310, South Korea
[2] Korea Polar Res Inst, Res Unit Cryogen Novel Mat, Incheon 07505, South Korea
[3] Univ Sci & Technol, Dept Polar Sci, Incheon 07505, South Korea
[4] Sungkyunkwan Univ, Grad Sch Basic Med Sci GSBMS, Dept Precis Med, Sch Med, Suwon 16419, South Korea
[5] Korea Polar Res Inst, Div Life Sci, Incheon 07505, South Korea
关键词
crystal structure; LaFae; ferulic acid; feruloyl esterase; X-ray crystallography; CINNAMOYL ESTERASES; XYLANASE; PURIFICATION; ENZYMES; OIL;
D O I
10.3390/ijms241311170
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 (LaFae) from Lactobacillus acidophilus. Our results demonstrated that LaFae 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 LaFae enzymatic hydrolysis, thereby augmenting ferulic acid production. To further investigate the active site configuration of LaFae, crystal structures of unliganded and ethyl ferulate-bound LaFae were determined at 2.3 and 2.19 & ANGS; 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 LaFae activity against p-nitrophenyl butyrate. Our results highlight the considerable application potential of LaFae to produce ferulic acid from plant biomass and agricultural by-products.
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页数:17
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