Insights into ferulic acid detoxification mechanism by using a novel adsorbent, AEPA250: The microinteraction of ferulic acid with AEPA250 and Saccharomyces cerevisiae

2021 ◽  
Vol 415 ◽  
pp. 125685
Author(s):  
Jinju Hou ◽  
Shudong Zhang ◽  
Xiaotong Zhang ◽  
Kainan Wang ◽  
Qiuzhuo Zhang ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ferulic Acid ◽  
Detoxification Mechanism

scholarly journals Biotransformation of ferulic acid by the phytopathogenic fungi Colletotrichum acutatum and Lasiodiplodia theobromae

2016 ◽  
Vol 69 (1) ◽  
pp. 7835-7844 ◽  
Author(s):  
Manuel Alejandro Numpaque ◽  
Jesús Humberto Gil González ◽  
Diego Luis Durango Restrepo
Keyword(s):  
Ferulic Acid ◽  
Culture Medium ◽  
Microbial Transformation ◽  
Phytopathogenic Fungi ◽  
Colletotrichum Acutatum ◽  
Lasiodiplodia Theobromae ◽  
Natural Production ◽  
Total Inhibition ◽  
Detoxification Mechanism ◽  
Economical Alternative

The microbial transformation of ferulic acid (FA) offers a cleaner, more economical alternative for the natural production of flavorings and fragrances. In the present study, the biotransformation of FA using the filamentous phytopathogenic fungi Colletotrichum acutatum and Lasiodiplodia theobromae was researched. Initially, the toxicity of FA against both fungi was evaluated; the FA displayed a moderate toxicity (total inhibition at concentrations ≥ 2000 mg L-1) and apparently a detoxification mechanism was present. Afterwards, the microorganisms were incubated with the substrate at room conditions using a Czapek-Dox culture medium. The results demonstrated that the FA was mainly converted to 4-vinylguaiacol, reaching the highest abundance within the first 48 hours. To a lesser extent, acetovanillone, ethylguaiacol, and vanillin, among others, were produced. Interestingly, the compounds generated in the biotransformation of FA with C. acutatum and L. theobromae have been used as flavorings. Based on the identified metabolites, a possible metabolic pathway was proposed.

scholarly journals Pregnenolone esterification in Saccharomyces cerevisiae . A potential detoxification mechanism

1999 ◽  
Vol 261 (1) ◽  
pp. 317-324 ◽  
Author(s):  
Gilles Cauet ◽  
Eric Degryse ◽  
Catherine Ledoux ◽  
Roberto Spagnoli ◽  
Tilman Achstetter
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Detoxification Mechanism

scholarly journals Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Emma Zsófia Aletta Nagy ◽  
Csaba Levente Nagy ◽  
Alina Filip ◽  
Katalin Nagy ◽  
Emese Gál ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ferulic Acid ◽  
Acid Decarboxylase ◽  
Ferulic Acid Decarboxylase

Engineering Saccharomyces cerevisiae to produce feruloyl esterase for the release of ferulic acid from switchgrass

2011 ◽  
Vol 38 (12) ◽  
pp. 1961-1967 ◽  
Author(s):  
Dominic W. S. Wong ◽  
Victor J. Chan ◽  
Sarah B. Batt ◽  
Gautam Sarath ◽  
Hans Liao
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ferulic Acid ◽  
Feruloyl Esterase

scholarly journals Structure and Mechanism of Ferulic Acid Decarboxylase (FDC1) from Saccharomyces cerevisiae

2015 ◽  
Vol 81 (12) ◽  
pp. 4216-4223 ◽  
Author(s):  
Mohammad Wadud Bhuiya ◽  
Soon Goo Lee ◽  
Joseph M. Jez ◽  
Oliver Yu
Keyword(s):  
Crystal Structure ◽  
Saccharomyces Cerevisiae ◽  
Ferulic Acid ◽  
Active Site ◽  
Three Dimensional ◽  
Structural Similarity ◽  
Dimensional Structure ◽  
Acid Decarboxylase ◽  
Content Type ◽  
Ferulic Acid Decarboxylase

ABSTRACTThe nonoxidative decarboxylation of aromatic acids occurs in a range of microbes and is of interest for bioprocessing and metabolic engineering. Although phenolic acid decarboxylases provide useful tools for bioindustrial applications, the molecular bases for how these enzymes function are only beginning to be examined. Here we present the 2.35-Å-resolution X-ray crystal structure of the ferulic acid decarboxylase (FDC1; UbiD) fromSaccharomyces cerevisiae. FDC1 shares structural similarity with the UbiD family of enzymes that are involved in ubiquinone biosynthesis. The position of 4-vinylphenol, the product ofp-coumaric acid decarboxylation, in the structure identifies a large hydrophobic cavity as the active site. Differences in the β2e-α5 loop of chains in the crystal structure suggest that the conformational flexibility of this loop allows access to the active site. The structure also implicates Glu285 as the general base in the nonoxidative decarboxylation reaction catalyzed by FDC1. Biochemical analysis showed a loss of enzymatic activity in the E285A mutant. Modeling of 3-methoxy-4-hydroxy-5-decaprenylbenzoate, a partial structure of the physiological UbiD substrate, in the binding site suggests that an ∼30-Å-long pocket adjacent to the catalytic site may accommodate the isoprenoid tail of the substrate needed for ubiquinone biosynthesis in yeast. The three-dimensional structure of yeast FDC1 provides a template for guiding protein engineering studies aimed at optimizing the efficiency of aromatic acid decarboxylation reactions in bioindustrial applications.

scholarly journals Catabolism of coniferyl aldehyde, ferulic acid and p-coumaric acid by Saccharomyces cerevisiae yields less toxic products

2015 ◽  
Vol 14 (1) ◽  
Author(s):  
Peter Temitope Adeboye ◽  
Maurizio Bettiga ◽  
Fredrik Aldaeus ◽  
Per Tomas Larsson ◽  
Lisbeth Olsson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ferulic Acid ◽  
Coumaric Acid

Curcumin biosynthesis from ferulic acid by engineered Saccharomyces cerevisiae

2021 ◽  
pp. 2100400
Author(s):  
João Rainha ◽  
Joana L. Rodrigues ◽  
Cristiana Faria ◽  
Lígia R. Rodrigues
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ferulic Acid ◽  
Engineered Saccharomyces Cerevisiae
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