scholarly journals Generation of 4-vinylguaiacol through a novel high-affinity ferulic acid decarboxylase to obtain smoke flavours without carcinogenic contaminants

PLoS ONE ◽  
2020 ◽  
Vol 15 (12) ◽  
pp. e0244290
Author(s):  
Thorben Detering ◽  
Katharina Mundry ◽  
Ralf G. Berger
Keyword(s):  
Ferulic Acid ◽  
Schizophyllum Commune ◽  
Catalytic Efficiency ◽  
Acid Decarboxylase ◽  
Turnover Number ◽  
High Affinity ◽  
Sequence Identity ◽  
Ferulic Acid Decarboxylase ◽  
New Generation ◽  
The Impact

Traditional smoke flavours bear the risk of containing a multitude of contaminating carcinogenic side-products. Enzymatic decarboxylation of ferulic acid released from agro-industrial side-streams by ferulic acid esterases (FAE) enables the sustainable generation of pure, food grade 4-vinylguaiacol (4-VG), the impact compound of smoke flavour. The first basidiomycetous ferulic acid decarboxylase (FAD) was isolated from Schizophyllum commune (ScoFAD) and heterologously produced by Komagataella phaffii. It showed a molecular mass of 21 kDa, catalytic optima at pH 5.5 and 35°C, and a sequence identity of 63.6% to its next relative, a FAD from the ascomycete Cordyceps farinosa. The ScoFAD exhibited a high affinity to its only known substrate ferulic acid (FA) of 0.16 mmol L-1 and a turnover number of 750 s-1. The resulting catalytic efficiency kcat KM-1 of 4,779 L s-1 mmol-1 exceeded the next best known enzyme by more than a factor of 50. Immobilised on AminoLink Plus Agarose, ScoFAD maintained its activity for several days. The combination with FAEs and agro-industrial side-streams paves the way for a new generation of sustainable, clean, and safe smoke flavours.

Chemoenzymatic cascade for stilbene production from cinnamic acid catalyzed by ferulic acid decarboxylase and an artificial metathease

2019 ◽  
Vol 9 (20) ◽  
pp. 5572-5576 ◽  
Author(s):  
M. A. Stephanie Mertens ◽  
Daniel F. Sauer ◽  
Ulrich Markel ◽  
Johannes Schiffels ◽  
Jun Okuda ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Cinnamic Acid ◽  
Olefin Metathesis ◽  
Metal Contamination ◽  
Cascade Reaction ◽  
Acid Decarboxylase ◽  
Efficient Removal ◽  
Ferulic Acid Decarboxylase ◽  
Acid Catalyzed ◽  
Removal Of Metal

We report a chemoenzymatic cascade reaction for stilbene production combining decarboxylation and olefin metathesis with efficient removal of metal contamination.

Mechanistic insights into the catalytic reaction of ferulic acid decarboxylase from Aspergillus niger: a QM/MM study

2017 ◽  
Vol 19 (11) ◽  
pp. 7733-7742 ◽  
Author(s):  
Ge Tian ◽  
Yongjun Liu
Keyword(s):  
Aspergillus Niger ◽  
Ferulic Acid ◽  
Catalytic Reaction ◽  
Acid Decarboxylase ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Ferulic Acid Decarboxylase ◽  
Rate Limiting

QM/MM calculations reveal the cofactor prFMNiminiumto be the catalytically relevant species compared with prFMNketamine. The protonation of the intermediate is the rate-limiting step, and the prolonged leaving of the generated CO2can facilitate this process.

scholarly journals Structural Basis of Enzymatic Activity for the Ferulic Acid Decarboxylase (FADase) from Enterobacter sp. Px6-4

PLoS ONE ◽  
2011 ◽  
Vol 6 (1) ◽  
pp. e16262 ◽  
Author(s):  
Wen Gu ◽  
Jinkui Yang ◽  
Zhiyong Lou ◽  
Lianming Liang ◽  
Yuna Sun ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Ferulic Acid ◽  
Structural Basis ◽  
Acid Decarboxylase ◽  
Ferulic Acid Decarboxylase

Cloning, sequencing, and overexpression in Escherichia coli of the Enterobacter sp. Px6-4 gene for ferulic acid decarboxylase

2010 ◽  
Vol 89 (6) ◽  
pp. 1797-1805 ◽  
Author(s):  
Wen Gu ◽  
Xuemei Li ◽  
Jingwen Huang ◽  
Yanqing Duan ◽  
Zhaohui Meng ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ferulic Acid ◽  
Acid Decarboxylase ◽  
Ferulic Acid Decarboxylase

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

Isofunctional Enzymes PAD1 and UbiX Catalyze Formation of a Novel Cofactor Required by Ferulic Acid Decarboxylase and 4-Hydroxy-3-polyprenylbenzoic Acid Decarboxylase

2015 ◽  
Vol 10 (4) ◽  
pp. 1137-1144 ◽  
Author(s):  
Fengming Lin ◽  
Kyle L. Ferguson ◽  
David R. Boyer ◽  
Xiaoxia Nina Lin ◽  
E. Neil G. Marsh
Keyword(s):  
Ferulic Acid ◽  
Acid Decarboxylase ◽  
Ferulic Acid Decarboxylase

scholarly journals Direct 1,3-butadiene biosynthesis in Escherichia coli via a tailored ferulic acid decarboxylase mutant

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Yutaro Mori ◽  
Shuhei Noda ◽  
Tomokazu Shirai ◽  
Akihiko Kondo
Keyword(s):  
Escherichia Coli ◽  
Carbon Source ◽  
Ferulic Acid ◽  
Rational Design ◽  
Acid Decarboxylase ◽  
Enzyme Design ◽  
Muconic Acid ◽  
Synthetic Rubber ◽  
Ferulic Acid Decarboxylase ◽  
Fed Batch Fermentation

AbstractThe C4 unsaturated compound 1,3-butadiene is an important monomer in synthetic rubber and engineering plastic production. However, microorganisms cannot directly produce 1,3-butadiene when glucose is used as a renewable carbon source via biological processes. In this study, we construct an artificial metabolic pathway for 1,3-butadiene production from glucose in Escherichia coli by combining the cis,cis-muconic acid (ccMA)-producing pathway together with tailored ferulic acid decarboxylase mutations. The rational design of the substrate-binding site of the enzyme by computational simulations improves ccMA decarboxylation and thus 1,3-butadiene production. We find that changing dissolved oxygen (DO) levels and controlling the pH are important factors for 1,3-butadiene production. Using DO–stat fed-batch fermentation, we produce 2.13 ± 0.17 g L−1 1,3-butadiene. The results indicate that we can produce unnatural/nonbiological compounds from glucose as a renewable carbon source via a rational enzyme design strategy.

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