Improved Alkyl Glycoside Synthesis by trans‐Glycosylation through Tailored Microenvironments of Immobilized β‐Glucosidase

Christian Hoffmann, Carl Grey, Manuel Pinelo, John M. Woodley, Anders E. Daugaard*, Patrick Adlercreutz

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Here, we present for the first time, how the micro‐environment can directly improve biocatalytic selectivity of immobilized ß‐glucosidase. ß‐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 ß‐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.
Original languageEnglish
JournalChemPlusChem
ISSN2192-6506
DOIs
Publication statusAccepted/In press - 2019

Cite this

@article{6ec8302e37cb47148449492fd980b778,
title = "Improved Alkyl Glycoside Synthesis by trans‐Glycosylation through Tailored Microenvironments of Immobilized β‐Glucosidase",
abstract = "Here, we present for the first time, how the micro‐environment can directly improve biocatalytic selectivity of immobilized {\ss}‐glucosidase. {\ss}‐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 {\ss}‐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.",
author = "Christian Hoffmann and Carl Grey and Manuel Pinelo and Woodley, {John M.} and Daugaard, {Anders E.} and Patrick Adlercreutz",
year = "2019",
doi = "10.1002/cplu.201900680",
language = "English",
journal = "ChemPlusChem",
issn = "2192-6506",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",

}

Improved Alkyl Glycoside Synthesis by trans‐Glycosylation through Tailored Microenvironments of Immobilized β‐Glucosidase. / Hoffmann, Christian; Grey, Carl; Pinelo, Manuel; Woodley, John M.; Daugaard, Anders E.; Adlercreutz, Patrick.

In: ChemPlusChem, 2019.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Improved Alkyl Glycoside Synthesis by trans‐Glycosylation through Tailored Microenvironments of Immobilized β‐Glucosidase

AU - Hoffmann, Christian

AU - Grey, Carl

AU - Pinelo, Manuel

AU - Woodley, John M.

AU - Daugaard, Anders E.

AU - Adlercreutz, Patrick

PY - 2019

Y1 - 2019

N2 - Here, we present for the first time, how the micro‐environment can directly improve biocatalytic selectivity of immobilized ß‐glucosidase. ß‐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 ß‐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.

AB - Here, we present for the first time, how the micro‐environment can directly improve biocatalytic selectivity of immobilized ß‐glucosidase. ß‐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 ß‐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.

U2 - 10.1002/cplu.201900680

DO - 10.1002/cplu.201900680

M3 - Journal article

JO - ChemPlusChem

JF - ChemPlusChem

SN - 2192-6506

ER -