Details
| Original language | English |
|---|---|
| Pages (from-to) | 8497-8506 |
| Number of pages | 10 |
| Journal | ACS Sustainable Chemistry and Engineering |
| Volume | 9 |
| Issue number | 25 |
| Early online date | 11 Jun 2021 |
| Publication status | Published - 28 Jun 2021 |
| Externally published | Yes |
Abstract
The eobiotic compound indican lends itself to a compelling biocatalytic dyeing strategy for denim, in which the formation of corrosive byproducts is avoided. However, the efficient and scalable production of indican remains a key bottleneck. This work focuses on the in vitro characterization of PtUGT1, a glycosyltransferase from Polygonum tinctorium that catalyzes the formation of indican via the glycosylation of indoxyl. Here, the buffer composition and enzyme concentration were identified as key parameters for enzyme activity and stability. The short lifetime of the enzyme under reaction conditions initiated an immobilization study. As a consequence, an amino-functionalized methacrylate resin was identified as a highly functional option for efficient immobilization of PtUGT1, allowing immobilization yields of >98% for enzyme loadings up to 7.6 wt %. We further report a stabilization factor of 47 and significantly improved overall biocatalytic productivity. The straightforward handling and reuse of the described heterogeneous biocatalyst is demonstrated.
Keywords
- Bioprocess engineering, Denim dyes, Enzyme immobilization, Glycosylation, Glycosyltransferase, Green manufacturing
ASJC Scopus subject areas
- Chemistry(all)
- Environmental Science(all)
- Environmental Chemistry
- Chemical Engineering(all)
- Energy(all)
- Renewable Energy, Sustainability and the Environment
Sustainable Development Goals
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In: ACS Sustainable Chemistry and Engineering, Vol. 9, No. 25, 28.06.2021, p. 8497-8506.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Exploring the in Vitro Operating Window of Glycosyltransferase PtUGT1 from Polygonum tinctorium for a Biocatalytic Route to Indigo Dye
AU - Petermeier, Philipp
AU - Fortuna, Cristina
AU - Hübschmann, Kathrine M.
AU - Bidart, Gonzalo N.
AU - Tørring, Thomas
AU - Teze, David
AU - Welner, Ditte H.
AU - Kara, Selin
N1 - Funding Information: This project has received funding from the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement no. 860414 and from The Novo Nordisk Foundation Grant number: NNF10CC1016517.
PY - 2021/6/28
Y1 - 2021/6/28
N2 - The eobiotic compound indican lends itself to a compelling biocatalytic dyeing strategy for denim, in which the formation of corrosive byproducts is avoided. However, the efficient and scalable production of indican remains a key bottleneck. This work focuses on the in vitro characterization of PtUGT1, a glycosyltransferase from Polygonum tinctorium that catalyzes the formation of indican via the glycosylation of indoxyl. Here, the buffer composition and enzyme concentration were identified as key parameters for enzyme activity and stability. The short lifetime of the enzyme under reaction conditions initiated an immobilization study. As a consequence, an amino-functionalized methacrylate resin was identified as a highly functional option for efficient immobilization of PtUGT1, allowing immobilization yields of >98% for enzyme loadings up to 7.6 wt %. We further report a stabilization factor of 47 and significantly improved overall biocatalytic productivity. The straightforward handling and reuse of the described heterogeneous biocatalyst is demonstrated.
AB - The eobiotic compound indican lends itself to a compelling biocatalytic dyeing strategy for denim, in which the formation of corrosive byproducts is avoided. However, the efficient and scalable production of indican remains a key bottleneck. This work focuses on the in vitro characterization of PtUGT1, a glycosyltransferase from Polygonum tinctorium that catalyzes the formation of indican via the glycosylation of indoxyl. Here, the buffer composition and enzyme concentration were identified as key parameters for enzyme activity and stability. The short lifetime of the enzyme under reaction conditions initiated an immobilization study. As a consequence, an amino-functionalized methacrylate resin was identified as a highly functional option for efficient immobilization of PtUGT1, allowing immobilization yields of >98% for enzyme loadings up to 7.6 wt %. We further report a stabilization factor of 47 and significantly improved overall biocatalytic productivity. The straightforward handling and reuse of the described heterogeneous biocatalyst is demonstrated.
KW - Bioprocess engineering
KW - Denim dyes
KW - Enzyme immobilization
KW - Glycosylation
KW - Glycosyltransferase
KW - Green manufacturing
UR - http://www.scopus.com/inward/record.url?scp=85108639689&partnerID=8YFLogxK
U2 - 10.1021/acssuschemeng.1c01536
DO - 10.1021/acssuschemeng.1c01536
M3 - Article
AN - SCOPUS:85108639689
VL - 9
SP - 8497
EP - 8506
JO - ACS Sustainable Chemistry and Engineering
JF - ACS Sustainable Chemistry and Engineering
SN - 2168-0485
IS - 25
ER -