Horseradish peroxidase (HRP) was biotinylated with biotinamidocaproate N-hydroxysuccinimide ester (BcapNHS) in a controlled manner to obtain biotinylated horseradish peroxidase (Bcap-HRP) with two biotin moieties per enzyme molecule. Avidin-mediated immobilization of HRP was achieved by first coupli
Removal of chlorophenols from wastewater by immobilized horseradish peroxidase
โ Scribed by Kenji Tatsumi; Shinji Wada; Hiroyasu Ichikawa
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 533 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0006-3592
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โฆ Synopsis
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-trichlorophenoI, 2,4,6-trichlorophenoI, 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 chlorophe-no1 could not be attained, and in particular, the removal of 2,4,5-trichlorophenol was the lowest, with a removal rate of only 36%.
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