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Title: Poly(ethylene glycol)-modified ligninase enhances pentachlorophenol biodegradation in water-solvent mixtures

Abstract

Polychlorinated hydrocarbons are prevalent environmental contaminants whose rates of biodegradation are limited by their minimal solubilities in aqueous solutions where the biological reactions take place. In this study, ligninase (LiP) from Phanerochaete chrysosporium was modified by poly(ethylene glycol) to enhance its activity and stability for the biodegradation of pentachlorophenol (PCP) in the presence of acetonitrile (MeCN), a water-miscible solvent. The modified enzyme retained 100% of its activity in aqueous solutions and showed enhanced tolerance against the organic solvent. The activity of the modified enzyme was found to be over twice that of the native enzyme in the presence of 10% (v/v) MeCN. The solubility of PCP was enhanced significantly by the addition of MeCN to aqueous solutions, such that it was over 10-fold more soluble in the presence of 15% (v/v) MeCN than in pure aqueous buffer solution. Capitalizing on the enhanced substrate solubility and the increased activity of the modified enzyme, the catalytic efficiency of the modified LiP in solutions containing 15% MeCN was over 11-fold higher than that of the native enzyme in buffer solutions in unoptimized reactor systems. Continued research both in the use of organic solvents to increase the availability of recalcitrant contaminants and in themore » modification of enzymes to enhance their activity and stability in such solvents promises to dramatically affect their ability to remediate contaminated sites.« less

Authors:
; ;  [1]
  1. (Oak Ridge National Lab., TN (United States). Chemical Technology Div.)
Publication Date:
OSTI Identifier:
6299439
Resource Type:
Journal Article
Journal Name:
Biotechnology and Bioengineering
Additional Journal Information:
Journal Volume: 64:3; Journal ID: ISSN 0006-3592
Country of Publication:
United States
Language:
English
Subject:
54 ENVIRONMENTAL SCIENCES; BIODEGRADATION; CELLULASE; CHLORINATED AROMATIC HYDROCARBONS; ENZYME ACTIVITY; ORGANIC SOLVENTS; POLYETHYLENE GLYCOLS; REMEDIAL ACTION; ALCOHOLS; AROMATICS; CHEMICAL REACTIONS; DECOMPOSITION; ENZYMES; GLYCOLS; GLYCOSYL HYDROLASES; HALOGENATED AROMATIC HYDROCARBONS; HYDROLASES; HYDROXY COMPOUNDS; O-GLYCOSYL HYDROLASES; ORGANIC CHLORINE COMPOUNDS; ORGANIC COMPOUNDS; ORGANIC HALOGEN COMPOUNDS; ORGANIC POLYMERS; POLYMERS; PROTEINS; SOLVENTS; 540220* - Environment, Terrestrial- Chemicals Monitoring & Transport- (1990-)

Citation Formats

Wang, P., Woodward, C.A., and Kaufman, E.N. Poly(ethylene glycol)-modified ligninase enhances pentachlorophenol biodegradation in water-solvent mixtures. United States: N. p., 1999. Web. doi:10.1002/(SICI)1097-0290(19990805)64:3<290::AID-BIT5>3.0.CO;2-K.
Wang, P., Woodward, C.A., & Kaufman, E.N. Poly(ethylene glycol)-modified ligninase enhances pentachlorophenol biodegradation in water-solvent mixtures. United States. doi:10.1002/(SICI)1097-0290(19990805)64:3<290::AID-BIT5>3.0.CO;2-K.
Wang, P., Woodward, C.A., and Kaufman, E.N. Thu . "Poly(ethylene glycol)-modified ligninase enhances pentachlorophenol biodegradation in water-solvent mixtures". United States. doi:10.1002/(SICI)1097-0290(19990805)64:3<290::AID-BIT5>3.0.CO;2-K.
@article{osti_6299439,
title = {Poly(ethylene glycol)-modified ligninase enhances pentachlorophenol biodegradation in water-solvent mixtures},
author = {Wang, P. and Woodward, C.A. and Kaufman, E.N.},
abstractNote = {Polychlorinated hydrocarbons are prevalent environmental contaminants whose rates of biodegradation are limited by their minimal solubilities in aqueous solutions where the biological reactions take place. In this study, ligninase (LiP) from Phanerochaete chrysosporium was modified by poly(ethylene glycol) to enhance its activity and stability for the biodegradation of pentachlorophenol (PCP) in the presence of acetonitrile (MeCN), a water-miscible solvent. The modified enzyme retained 100% of its activity in aqueous solutions and showed enhanced tolerance against the organic solvent. The activity of the modified enzyme was found to be over twice that of the native enzyme in the presence of 10% (v/v) MeCN. The solubility of PCP was enhanced significantly by the addition of MeCN to aqueous solutions, such that it was over 10-fold more soluble in the presence of 15% (v/v) MeCN than in pure aqueous buffer solution. Capitalizing on the enhanced substrate solubility and the increased activity of the modified enzyme, the catalytic efficiency of the modified LiP in solutions containing 15% MeCN was over 11-fold higher than that of the native enzyme in buffer solutions in unoptimized reactor systems. Continued research both in the use of organic solvents to increase the availability of recalcitrant contaminants and in the modification of enzymes to enhance their activity and stability in such solvents promises to dramatically affect their ability to remediate contaminated sites.},
doi = {10.1002/(SICI)1097-0290(19990805)64:3<290::AID-BIT5>3.0.CO;2-K},
journal = {Biotechnology and Bioengineering},
issn = {0006-3592},
number = ,
volume = 64:3,
place = {United States},
year = {1999},
month = {8}
}