Stabilization of activity of cellulase and hemicellulase enzymes by covering with polyacrylamide layer

Imre Hegedus, E. Nagy

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Enzymes (β-d-xylosidase, endoxylanase and endocellulase), isolated from Thermobifida fusca moderate thermophile organism, have been stabilized as single enzyme nanoparticles. During the stabilization process every individual enzyme molecule is covered with a thin polyacrylamide polymer layer. This polymer layer has a cross-linked spatial structure but thin and porous enough to allow the diffusion of substrate molecules to the active centrum of the enzyme molecule and the enzymatic function of the pretreated enzyme. A new, easily realizable two-step process was used to prepare enzyme nanoparticles. The catalytic activity of these three native enzymes and enzyme nanoparticles prepared were measured as a function of the incubation time, with 150. rpm shaking at 50°C as optimal temperature. All enzymes are significantly more stable in form of enzyme nanoparticles than in their natural state. Heat stability of β-d-xylosidase enzyme was also investigated at 80°C and 150rpm. The half-life time of activity of enzyme nanoparticles obtained was about two-order of magnitude longer than that of the natural ones.

Original languageEnglish
Pages (from-to)143-150
Number of pages8
JournalChemical Engineering and Processing: Process Intensification
Volume95
DOIs
Publication statusPublished - 2015

Fingerprint

Cellulase
Polyacrylates
Enzymes
Stabilization
Nanoparticles
Xylosidases
Molecules
polyacrylamide
hemicellulase
Polymers
Endo-1,4-beta Xylanases
Cellulases
Catalyst activity

Keywords

  • Enzyme stabilization
  • Heat stability
  • Second generation bioethanol production
  • Single enzyme nanoparticles

ASJC Scopus subject areas

  • Chemical Engineering(all)
  • Chemistry(all)
  • Industrial and Manufacturing Engineering
  • Energy Engineering and Power Technology

Cite this

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title = "Stabilization of activity of cellulase and hemicellulase enzymes by covering with polyacrylamide layer",
abstract = "Enzymes (β-d-xylosidase, endoxylanase and endocellulase), isolated from Thermobifida fusca moderate thermophile organism, have been stabilized as single enzyme nanoparticles. During the stabilization process every individual enzyme molecule is covered with a thin polyacrylamide polymer layer. This polymer layer has a cross-linked spatial structure but thin and porous enough to allow the diffusion of substrate molecules to the active centrum of the enzyme molecule and the enzymatic function of the pretreated enzyme. A new, easily realizable two-step process was used to prepare enzyme nanoparticles. The catalytic activity of these three native enzymes and enzyme nanoparticles prepared were measured as a function of the incubation time, with 150. rpm shaking at 50°C as optimal temperature. All enzymes are significantly more stable in form of enzyme nanoparticles than in their natural state. Heat stability of β-d-xylosidase enzyme was also investigated at 80°C and 150rpm. The half-life time of activity of enzyme nanoparticles obtained was about two-order of magnitude longer than that of the natural ones.",
keywords = "Enzyme stabilization, Heat stability, Second generation bioethanol production, Single enzyme nanoparticles",
author = "Imre Hegedus and E. Nagy",
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journal = "Chemical Engineering and Processing - Process Intensification",
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T1 - Stabilization of activity of cellulase and hemicellulase enzymes by covering with polyacrylamide layer

AU - Hegedus, Imre

AU - Nagy, E.

PY - 2015

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N2 - Enzymes (β-d-xylosidase, endoxylanase and endocellulase), isolated from Thermobifida fusca moderate thermophile organism, have been stabilized as single enzyme nanoparticles. During the stabilization process every individual enzyme molecule is covered with a thin polyacrylamide polymer layer. This polymer layer has a cross-linked spatial structure but thin and porous enough to allow the diffusion of substrate molecules to the active centrum of the enzyme molecule and the enzymatic function of the pretreated enzyme. A new, easily realizable two-step process was used to prepare enzyme nanoparticles. The catalytic activity of these three native enzymes and enzyme nanoparticles prepared were measured as a function of the incubation time, with 150. rpm shaking at 50°C as optimal temperature. All enzymes are significantly more stable in form of enzyme nanoparticles than in their natural state. Heat stability of β-d-xylosidase enzyme was also investigated at 80°C and 150rpm. The half-life time of activity of enzyme nanoparticles obtained was about two-order of magnitude longer than that of the natural ones.

AB - Enzymes (β-d-xylosidase, endoxylanase and endocellulase), isolated from Thermobifida fusca moderate thermophile organism, have been stabilized as single enzyme nanoparticles. During the stabilization process every individual enzyme molecule is covered with a thin polyacrylamide polymer layer. This polymer layer has a cross-linked spatial structure but thin and porous enough to allow the diffusion of substrate molecules to the active centrum of the enzyme molecule and the enzymatic function of the pretreated enzyme. A new, easily realizable two-step process was used to prepare enzyme nanoparticles. The catalytic activity of these three native enzymes and enzyme nanoparticles prepared were measured as a function of the incubation time, with 150. rpm shaking at 50°C as optimal temperature. All enzymes are significantly more stable in form of enzyme nanoparticles than in their natural state. Heat stability of β-d-xylosidase enzyme was also investigated at 80°C and 150rpm. The half-life time of activity of enzyme nanoparticles obtained was about two-order of magnitude longer than that of the natural ones.

KW - Enzyme stabilization

KW - Heat stability

KW - Second generation bioethanol production

KW - Single enzyme nanoparticles

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