Immobilization of alcohol dehydrogenase on ceramic silicon carbide membranes for enzymatic CH3 OH production

Birgitte Zeuner, Nicolaj Ma, Kasper Berendt, Anne S. Meyer, Pavle Andric, Jan Hoffmann Jørgensen, Manuel Pinelo*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

BACKGROUND Alcohol dehydrogenase (ADH; EC 1.1.1.1) catalyzes oxidation of CH3OH to CHOH during NAD+ reduction to NADH. ADH can also accelerate the reverse reaction, which is studied as part of cascadic enzymatic conversion of CO2 to CH3OH. In the present study, immobilization of ADH onto macroporous membranes of silicon carbide (SiC) was investigated for CHOH to CH3OH conversion.

RESULTS Immobilization techniques included physical adsorption directly to the membrane and functionalization of the membrane with polyethylenimine (PEI) or (3‐aminopropyl)triethoxysilane (APTES) followed by glutaraldehyde (GA) cross‐linking. Enzyme loadings, flux, NADH conversion, and overall ADH reusability were assessed. Enzyme loadings were similar, but substrate conversion was approximately 2 and 2.5 times higher for APTES‐GA and PEI‐GA, respectively, and the relative activity retention was better than for physical adsorption. Membrane surface treatment with NaOH prior to APTES‐GA immobilization resulted in significant improvement in enzyme loading and a doubling of ADH activity as well as higher activity during recycling as the ADH destabilization rate was unaffected.

CONCLUSIONS The results provided proof‐of‐concept for the use of NaOH‐treated SiC membranes for covalent enzyme immobilization and biocatalytic efficiency improvement of ADH during multiple reaction cycles. These data have implications for the development of robust extended enzymatic reactions.
Original languageEnglish
JournalJournal of Chemical Technology and Biotechnology
Volume93
Issue number10
Pages (from-to)2952-2961
ISSN0268-2575
DOIs
Publication statusPublished - 2018

Keywords

  • Alcohol dehydrogenase
  • Enzyme immobilization
  • Membrane technology
  • Silicon carbide
  • (3‐aminopropyl)triethoxysilane
  • Polyethylenimine
  • Physical adsorption

Cite this

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title = "Immobilization of alcohol dehydrogenase on ceramic silicon carbide membranes for enzymatic CH3 OH production",
abstract = "BACKGROUND Alcohol dehydrogenase (ADH; EC 1.1.1.1) catalyzes oxidation of CH3OH to CHOH during NAD+ reduction to NADH. ADH can also accelerate the reverse reaction, which is studied as part of cascadic enzymatic conversion of CO2 to CH3OH. In the present study, immobilization of ADH onto macroporous membranes of silicon carbide (SiC) was investigated for CHOH to CH3OH conversion.RESULTS Immobilization techniques included physical adsorption directly to the membrane and functionalization of the membrane with polyethylenimine (PEI) or (3‐aminopropyl)triethoxysilane (APTES) followed by glutaraldehyde (GA) cross‐linking. Enzyme loadings, flux, NADH conversion, and overall ADH reusability were assessed. Enzyme loadings were similar, but substrate conversion was approximately 2 and 2.5 times higher for APTES‐GA and PEI‐GA, respectively, and the relative activity retention was better than for physical adsorption. Membrane surface treatment with NaOH prior to APTES‐GA immobilization resulted in significant improvement in enzyme loading and a doubling of ADH activity as well as higher activity during recycling as the ADH destabilization rate was unaffected.CONCLUSIONS The results provided proof‐of‐concept for the use of NaOH‐treated SiC membranes for covalent enzyme immobilization and biocatalytic efficiency improvement of ADH during multiple reaction cycles. These data have implications for the development of robust extended enzymatic reactions.",
keywords = "Alcohol dehydrogenase, Enzyme immobilization, Membrane technology, Silicon carbide, (3‐aminopropyl)triethoxysilane, Polyethylenimine, Physical adsorption",
author = "Birgitte Zeuner and Nicolaj Ma and Kasper Berendt and Meyer, {Anne S.} and Pavle Andric and J{\o}rgensen, {Jan Hoffmann} and Manuel Pinelo",
year = "2018",
doi = "10.1002/jctb.5653",
language = "English",
volume = "93",
pages = "2952--2961",
journal = "Journal of Chemical Technology and Biotechnology",
issn = "0268-2575",
publisher = "JohnWiley & Sons Ltd.",
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}

Immobilization of alcohol dehydrogenase on ceramic silicon carbide membranes for enzymatic CH3 OH production. / Zeuner, Birgitte; Ma, Nicolaj; Berendt, Kasper; Meyer, Anne S.; Andric, Pavle; Jørgensen, Jan Hoffmann; Pinelo, Manuel.

In: Journal of Chemical Technology and Biotechnology, Vol. 93, No. 10, 2018, p. 2952-2961.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Immobilization of alcohol dehydrogenase on ceramic silicon carbide membranes for enzymatic CH3 OH production

AU - Zeuner, Birgitte

AU - Ma, Nicolaj

AU - Berendt, Kasper

AU - Meyer, Anne S.

AU - Andric, Pavle

AU - Jørgensen, Jan Hoffmann

AU - Pinelo, Manuel

PY - 2018

Y1 - 2018

N2 - BACKGROUND Alcohol dehydrogenase (ADH; EC 1.1.1.1) catalyzes oxidation of CH3OH to CHOH during NAD+ reduction to NADH. ADH can also accelerate the reverse reaction, which is studied as part of cascadic enzymatic conversion of CO2 to CH3OH. In the present study, immobilization of ADH onto macroporous membranes of silicon carbide (SiC) was investigated for CHOH to CH3OH conversion.RESULTS Immobilization techniques included physical adsorption directly to the membrane and functionalization of the membrane with polyethylenimine (PEI) or (3‐aminopropyl)triethoxysilane (APTES) followed by glutaraldehyde (GA) cross‐linking. Enzyme loadings, flux, NADH conversion, and overall ADH reusability were assessed. Enzyme loadings were similar, but substrate conversion was approximately 2 and 2.5 times higher for APTES‐GA and PEI‐GA, respectively, and the relative activity retention was better than for physical adsorption. Membrane surface treatment with NaOH prior to APTES‐GA immobilization resulted in significant improvement in enzyme loading and a doubling of ADH activity as well as higher activity during recycling as the ADH destabilization rate was unaffected.CONCLUSIONS The results provided proof‐of‐concept for the use of NaOH‐treated SiC membranes for covalent enzyme immobilization and biocatalytic efficiency improvement of ADH during multiple reaction cycles. These data have implications for the development of robust extended enzymatic reactions.

AB - BACKGROUND Alcohol dehydrogenase (ADH; EC 1.1.1.1) catalyzes oxidation of CH3OH to CHOH during NAD+ reduction to NADH. ADH can also accelerate the reverse reaction, which is studied as part of cascadic enzymatic conversion of CO2 to CH3OH. In the present study, immobilization of ADH onto macroporous membranes of silicon carbide (SiC) was investigated for CHOH to CH3OH conversion.RESULTS Immobilization techniques included physical adsorption directly to the membrane and functionalization of the membrane with polyethylenimine (PEI) or (3‐aminopropyl)triethoxysilane (APTES) followed by glutaraldehyde (GA) cross‐linking. Enzyme loadings, flux, NADH conversion, and overall ADH reusability were assessed. Enzyme loadings were similar, but substrate conversion was approximately 2 and 2.5 times higher for APTES‐GA and PEI‐GA, respectively, and the relative activity retention was better than for physical adsorption. Membrane surface treatment with NaOH prior to APTES‐GA immobilization resulted in significant improvement in enzyme loading and a doubling of ADH activity as well as higher activity during recycling as the ADH destabilization rate was unaffected.CONCLUSIONS The results provided proof‐of‐concept for the use of NaOH‐treated SiC membranes for covalent enzyme immobilization and biocatalytic efficiency improvement of ADH during multiple reaction cycles. These data have implications for the development of robust extended enzymatic reactions.

KW - Alcohol dehydrogenase

KW - Enzyme immobilization

KW - Membrane technology

KW - Silicon carbide

KW - (3‐aminopropyl)triethoxysilane

KW - Polyethylenimine

KW - Physical adsorption

U2 - 10.1002/jctb.5653

DO - 10.1002/jctb.5653

M3 - Journal article

VL - 93

SP - 2952

EP - 2961

JO - Journal of Chemical Technology and Biotechnology

JF - Journal of Chemical Technology and Biotechnology

SN - 0268-2575

IS - 10

ER -