Details
| Original language | English |
|---|---|
| Article number | 1700332 |
| Journal | Biotechnology journal |
| Volume | 12 |
| Issue number | 12 |
| Early online date | 1 Sept 2017 |
| Publication status | Published - Dec 2017 |
| Externally published | Yes |
Abstract
A variety of strategies is applied to alleviate thermodynamic and kinetic limitations in biocatalytic carboxylation of metabolites in vivo. A key feature to consider in enzymatic carboxylations is the nature of the cosubstrate: CO2 or its hydrated form, bicarbonate. The substrate binding and activation mechanism determine what the actual carboxylation agent is. Dihydroxybenzoic acid (de)carboxylases catalyze the reversible regio-selective ortho-(de)carboxylation of phenolics. These enzymes have attracted considerable attention in the last 10 years due to their potential in substituting harsh conditions typical of chemical carboxylations (100–200 °C, 5–100 bar) with, ideally, greener ones (20–40 °C, 1 bar). They are reported to use bicarbonate as substrate, needed in large excess to overcome thermodynamic and kinetic limitations. Therefore, CO2 can be used as substrate by these enzymes only if it is converted into bicarbonate in situ. In this contribution, we report the simultaneous amine-mediated conversion of CO2 into bicarbonate and the ortho-carboxylation of different phenolic molecules catalyzed by 2,3-dihydroxybenzoic acid (de)carboxylase from Aspergillus oryzae. Our results show that under the newly developed conditions a significant thermodynamic (up to twofold increase in conversion) and kinetic improvement (up to approx. fivefold increase in rate) of the biocatalytic carboxylation of catechol is achieved.
Keywords
- (de)carboxylases, 2-hydroxybenzoic acids, amine scrubbing, carboxylation, enzyme kinetics
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Medicine
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In: Biotechnology journal, Vol. 12, No. 12, 1700332, 12.2017.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Amine-Mediated Enzymatic Carboxylation of Phenols Using CO2 as Substrate Increases Equilibrium Conversions and Reaction Rates
AU - Pesci, Lorenzo
AU - Gurikov, Pavel
AU - Liese, Andreas
AU - Kara, Selin
PY - 2017/12
Y1 - 2017/12
N2 - A variety of strategies is applied to alleviate thermodynamic and kinetic limitations in biocatalytic carboxylation of metabolites in vivo. A key feature to consider in enzymatic carboxylations is the nature of the cosubstrate: CO2 or its hydrated form, bicarbonate. The substrate binding and activation mechanism determine what the actual carboxylation agent is. Dihydroxybenzoic acid (de)carboxylases catalyze the reversible regio-selective ortho-(de)carboxylation of phenolics. These enzymes have attracted considerable attention in the last 10 years due to their potential in substituting harsh conditions typical of chemical carboxylations (100–200 °C, 5–100 bar) with, ideally, greener ones (20–40 °C, 1 bar). They are reported to use bicarbonate as substrate, needed in large excess to overcome thermodynamic and kinetic limitations. Therefore, CO2 can be used as substrate by these enzymes only if it is converted into bicarbonate in situ. In this contribution, we report the simultaneous amine-mediated conversion of CO2 into bicarbonate and the ortho-carboxylation of different phenolic molecules catalyzed by 2,3-dihydroxybenzoic acid (de)carboxylase from Aspergillus oryzae. Our results show that under the newly developed conditions a significant thermodynamic (up to twofold increase in conversion) and kinetic improvement (up to approx. fivefold increase in rate) of the biocatalytic carboxylation of catechol is achieved.
AB - A variety of strategies is applied to alleviate thermodynamic and kinetic limitations in biocatalytic carboxylation of metabolites in vivo. A key feature to consider in enzymatic carboxylations is the nature of the cosubstrate: CO2 or its hydrated form, bicarbonate. The substrate binding and activation mechanism determine what the actual carboxylation agent is. Dihydroxybenzoic acid (de)carboxylases catalyze the reversible regio-selective ortho-(de)carboxylation of phenolics. These enzymes have attracted considerable attention in the last 10 years due to their potential in substituting harsh conditions typical of chemical carboxylations (100–200 °C, 5–100 bar) with, ideally, greener ones (20–40 °C, 1 bar). They are reported to use bicarbonate as substrate, needed in large excess to overcome thermodynamic and kinetic limitations. Therefore, CO2 can be used as substrate by these enzymes only if it is converted into bicarbonate in situ. In this contribution, we report the simultaneous amine-mediated conversion of CO2 into bicarbonate and the ortho-carboxylation of different phenolic molecules catalyzed by 2,3-dihydroxybenzoic acid (de)carboxylase from Aspergillus oryzae. Our results show that under the newly developed conditions a significant thermodynamic (up to twofold increase in conversion) and kinetic improvement (up to approx. fivefold increase in rate) of the biocatalytic carboxylation of catechol is achieved.
KW - (de)carboxylases
KW - 2-hydroxybenzoic acids
KW - amine scrubbing
KW - carboxylation
KW - enzyme kinetics
UR - http://www.scopus.com/inward/record.url?scp=85030226005&partnerID=8YFLogxK
U2 - 10.1002/biot.201700332
DO - 10.1002/biot.201700332
M3 - Article
C2 - 28862371
AN - SCOPUS:85030226005
VL - 12
JO - Biotechnology journal
JF - Biotechnology journal
SN - 1860-6768
IS - 12
M1 - 1700332
ER -