Removal of chlorophenols from wastewater by immobilized horseradish peroxidase

Journal Article · Fri Jul 05 04:00:00 EDT 1996 · Biotechnology and Bioengineering

DOI:https://doi.org/10.1002/(SICI)1097-0290(19960705)51:1<126::AID-BIT15>3.0.CO;2-O· OSTI ID:260444

Tatsumi, Kenji; Wada, Shinji; Ichikawa, Hiroyasu ^[1]

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1. National Inst. for Resources and Environment, Tsukuba, Ibaraki (Japan)

Immobilization of horseradish peroxidase on magnetite and removal of chlorophenols using immobilized enzyme were investigated. Immobilization by physical adsorption on magnetite was much more effective than that by the crosslinking method, and the enzyme was found to be immobilized at 100% of retained activity. In addition, it was discovered that horseradish peroxidase was selectively adsorbed on magnetite, and the immobilization resulted in a 20-fold purification rate for crude enzyme. When immobilized peroxidase was used to treat a solution containing various chlorophenols, p-chlorophenol, 2,4-dichlorophenol, 2,4,5-trichlorophenol, 2,4,6-trichlorophenol, 2,3,4,6-tetrachlorophenol, and pentachlorophenol, each chlorophenol was almost 100% removed, and also the removal of total organic carbon (TOC) and adsorbable organic halogen (AOX) reached more than 90%, respectively. However, in the case of soluble peroxidase, complete removal of each chlorophenol could not be attained, and in particular, the removal of 2,4,5-trichlorophenol was the lowest, with a removal rate of only 36%.

• OSTI ID: 260444
• Journal Information: Biotechnology and Bioengineering, Journal Name: Biotechnology and Bioengineering Journal Issue: 1 Vol. 51; ISSN BIBIAU; ISSN 0006-3592
• Country of Publication: United States
• Language: English

Related Subjects

54 ENVIRONMENTAL SCIENCES
BIODEGRADATION
CHLORINATED AROMATIC HYDROCARBONS
ENZYME ACTIVITY
IMMOBILIZED ENZYMES
PEROXIDASES