Improved Alkyl Glycoside Synthesis by trans-Glycosylation through Tailored Microenvironments of Immobilized β-Glucosidase
(2020) In ChemPlusChem 85(1). p.137-141- Abstract
We present how the microenvironment can directly improve biocatalytic selectivity of immobilized β-glucosidase. β-Glucosidase from Thermotoga neapolitana was immobilized on a variety of functionalized off-stoichiometric thiol-ene (OSTE) particles, where highest activities were observed for thiol and imidazole functional particles. Compared to the soluble enzyme, the selectivity (rs/rh) between trans-glycosylation of p-nitrophenyl β-D-glucopyranoside (pNPG) with 1-propanol over hydrolysis was increased by a factor of 2–3 using particles containing imidazole (rs/rh of 6.7) and carboxylic acid moieties (rs/rh of 9.2), respectively. These results demonstrate clearly that... (More)
We present how the microenvironment can directly improve biocatalytic selectivity of immobilized β-glucosidase. β-Glucosidase from Thermotoga neapolitana was immobilized on a variety of functionalized off-stoichiometric thiol-ene (OSTE) particles, where highest activities were observed for thiol and imidazole functional particles. Compared to the soluble enzyme, the selectivity (rs/rh) between trans-glycosylation of p-nitrophenyl β-D-glucopyranoside (pNPG) with 1-propanol over hydrolysis was increased by a factor of 2–3 using particles containing imidazole (rs/rh of 6.7) and carboxylic acid moieties (rs/rh of 9.2), respectively. These results demonstrate clearly that enzyme selectivity depends directly on the local environment of the enzyme with the support.
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- author
- Hoffmann, Christian ; Grey, Carl LU ; Pinelo, Manuel ; Woodley, John M. ; Daugaard, Anders E. and Adlercreutz, Patrick LU
- organization
- publishing date
- 2020-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- alkyl glycosides, enzyme immobilization, hydrolases, surface functionalization, trans-glycosylation
- in
- ChemPlusChem
- volume
- 85
- issue
- 1
- pages
- 5 pages
- publisher
- Institute of Organic Chemistry and Biochemistry
- external identifiers
-
- scopus:85079363126
- ISSN
- 2192-6506
- DOI
- 10.1002/cplu.201900680
- language
- English
- LU publication?
- yes
- id
- f0af92da-e0ef-41c0-99ab-eb8730c11f42
- date added to LUP
- 2020-02-28 11:22:18
- date last changed
- 2022-04-18 20:47:25
@article{f0af92da-e0ef-41c0-99ab-eb8730c11f42, abstract = {{<p>We present how the microenvironment can directly improve biocatalytic selectivity of immobilized β-glucosidase. β-Glucosidase from Thermotoga neapolitana was immobilized on a variety of functionalized off-stoichiometric thiol-ene (OSTE) particles, where highest activities were observed for thiol and imidazole functional particles. Compared to the soluble enzyme, the selectivity (r<sub>s</sub>/r<sub>h</sub>) between trans-glycosylation of p-nitrophenyl β-D-glucopyranoside (pNPG) with 1-propanol over hydrolysis was increased by a factor of 2–3 using particles containing imidazole (r<sub>s</sub>/r<sub>h</sub> of 6.7) and carboxylic acid moieties (r<sub>s</sub>/r<sub>h</sub> of 9.2), respectively. These results demonstrate clearly that enzyme selectivity depends directly on the local environment of the enzyme with the support.</p>}}, author = {{Hoffmann, Christian and Grey, Carl and Pinelo, Manuel and Woodley, John M. and Daugaard, Anders E. and Adlercreutz, Patrick}}, issn = {{2192-6506}}, keywords = {{alkyl glycosides; enzyme immobilization; hydrolases; surface functionalization; trans-glycosylation}}, language = {{eng}}, number = {{1}}, pages = {{137--141}}, publisher = {{Institute of Organic Chemistry and Biochemistry}}, series = {{ChemPlusChem}}, title = {{Improved Alkyl Glycoside Synthesis by trans-Glycosylation through Tailored Microenvironments of Immobilized β-Glucosidase}}, url = {{http://dx.doi.org/10.1002/cplu.201900680}}, doi = {{10.1002/cplu.201900680}}, volume = {{85}}, year = {{2020}}, }