Details
| Original language | English |
|---|---|
| Article number | 631 |
| Journal | CATALYSTS |
| Volume | 11 |
| Issue number | 5 |
| Publication status | Published - 14 May 2021 |
Abstract
Traditional smoking generates not only the impact flavor compound 4-vinylguaiacol, but concurrently many unwanted and potent toxic compounds such as polycyclic aromatic hydrocarbons. Enzyme technology provides a solution without any side-product formation. A feruloyl esterase from Rhizoctonia solani (RspCAE) liberated ferulic acid from low-priced sugar beet fiber. Decarboxylation of ferulic acid to 4-vinylguaiacol was achieved by a second enzyme from Schizophyllum commune (ScoFAD). Both enzymes were covalently immobilized on agarose to enable reusability in a fixed-bed approach. The two enzyme cascades showed high conversion rates with yields of 0.8 and 0.95, respectively, and retained activity for nearly 80 h of continuous operation. The overall productivity of the model process with bed volumes of 300 µL and a substrate flow rate of 0.25 mL min −1 was 3.98 mg 4-vinylguaiacol per hour. A cold online solid phase extraction using XAD4 was integrated into the bioprocess and provided high recovery rates during multiple elution steps. Attempting to facilitate the bioprocess, a fused gene coding for the two enzymes and a set of different linker lengths and properties was constructed and introduced into Komagataella phaffii. Longer and rigid linkers resulted in higher activity of the fusion protein with a maximum of 67 U L −1.
Keywords
- 4-vinylguaiacol, Basidiomycetes, Bioprocess, Fusion protein, Immobilization, Smoke flavor
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemistry(all)
- Physical and Theoretical Chemistry
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In: CATALYSTS, Vol. 11, No. 5, 631, 14.05.2021.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Alternative Routes for the Production of Natural 4-Vinylguaiacol from Sugar Beet Fiber Using Basidiomycetous Enzymes
AU - Günther, Thorben
AU - Schoppe, Lasse
AU - Ersoy, Franziska
AU - Berger, Ralf G.
N1 - Funding Information: Funding: This research was funded the BMBF cluster Rauchenzym, grant number 031B0586. The APC was funded by the Open Access fund of the Gottfried Wilhelm Leibniz Universität Hannover.
PY - 2021/5/14
Y1 - 2021/5/14
N2 - Traditional smoking generates not only the impact flavor compound 4-vinylguaiacol, but concurrently many unwanted and potent toxic compounds such as polycyclic aromatic hydrocarbons. Enzyme technology provides a solution without any side-product formation. A feruloyl esterase from Rhizoctonia solani (RspCAE) liberated ferulic acid from low-priced sugar beet fiber. Decarboxylation of ferulic acid to 4-vinylguaiacol was achieved by a second enzyme from Schizophyllum commune (ScoFAD). Both enzymes were covalently immobilized on agarose to enable reusability in a fixed-bed approach. The two enzyme cascades showed high conversion rates with yields of 0.8 and 0.95, respectively, and retained activity for nearly 80 h of continuous operation. The overall productivity of the model process with bed volumes of 300 µL and a substrate flow rate of 0.25 mL min −1 was 3.98 mg 4-vinylguaiacol per hour. A cold online solid phase extraction using XAD4 was integrated into the bioprocess and provided high recovery rates during multiple elution steps. Attempting to facilitate the bioprocess, a fused gene coding for the two enzymes and a set of different linker lengths and properties was constructed and introduced into Komagataella phaffii. Longer and rigid linkers resulted in higher activity of the fusion protein with a maximum of 67 U L −1.
AB - Traditional smoking generates not only the impact flavor compound 4-vinylguaiacol, but concurrently many unwanted and potent toxic compounds such as polycyclic aromatic hydrocarbons. Enzyme technology provides a solution without any side-product formation. A feruloyl esterase from Rhizoctonia solani (RspCAE) liberated ferulic acid from low-priced sugar beet fiber. Decarboxylation of ferulic acid to 4-vinylguaiacol was achieved by a second enzyme from Schizophyllum commune (ScoFAD). Both enzymes were covalently immobilized on agarose to enable reusability in a fixed-bed approach. The two enzyme cascades showed high conversion rates with yields of 0.8 and 0.95, respectively, and retained activity for nearly 80 h of continuous operation. The overall productivity of the model process with bed volumes of 300 µL and a substrate flow rate of 0.25 mL min −1 was 3.98 mg 4-vinylguaiacol per hour. A cold online solid phase extraction using XAD4 was integrated into the bioprocess and provided high recovery rates during multiple elution steps. Attempting to facilitate the bioprocess, a fused gene coding for the two enzymes and a set of different linker lengths and properties was constructed and introduced into Komagataella phaffii. Longer and rigid linkers resulted in higher activity of the fusion protein with a maximum of 67 U L −1.
KW - 4-vinylguaiacol
KW - Basidiomycetes
KW - Bioprocess
KW - Fusion protein
KW - Immobilization
KW - Smoke flavor
UR - http://www.scopus.com/inward/record.url?scp=85105728732&partnerID=8YFLogxK
U2 - 10.3390/catal11050631
DO - 10.3390/catal11050631
M3 - Article
VL - 11
JO - CATALYSTS
JF - CATALYSTS
SN - 2073-4344
IS - 5
M1 - 631
ER -