Jump to main content
US EPA
United States Environmental Protection Agency
Search
Search
Main menu
Environmental Topics
Laws & Regulations
About EPA
Health & Environmental Research Online (HERO)
Contact Us
Print
Feedback
Export to File
Search:
This record has one attached file:
Add More Files
Attach File(s):
Display Name for File*:
Save
Citation
Tags
HERO ID
2171169
Reference Type
Journal Article
Title
Degradation of polychlorinated biphenyls by extracellular enzymes of Phanerochaete chrysosporium produced in a perforated plate bioreactor
Author(s)
Krcmar, P; Kubatova, A; Votruba, J; Erbanova, P; Novotny, C; Sasek, V
Year
1999
Is Peer Reviewed?
1
Journal
World Journal of Microbiology and Biotechnology
ISSN:
0959-3993
EISSN:
1573-0972
Report Number
BIOSIS/00/28893
Volume
15
Issue
2
Page Numbers
269-276
Language
English
DOI
10.1023/A:1008994912875
Web of Science Id
WOS:000081082000015
Abstract
BIOSIS COPYRIGHT: BIOL ABS. The white rot fungus Phanerochaete chrysosporium was cultivated in a perforated plate bioreactor and the expression of activities of manganese-dependent peroxidase (MnP) and lignin peroxidase (LiP) was measured. Peak activities of the two enzymes were reached close to day 11 and therefore the cultivation was terminated on that day. Extracellular proteins were concentrated and both peroxidases separated by isoelectric focusing. Degradation of technical PCB mixtures containing low and highly chlor The degradation was not substrate-specific, because no significant differences between the respective degradation rates were observed with di-, tri-, tetra-, penta-, hexa-, hepta-, and octachlorinated congeners. In contrast, MnP and LiP isolated from the above-mentioned extracellular liquid did not catalyse any degradation.
Keywords
degradation; ligninolytic enzymes; polychlorinated biphenyls; white rot fungi
Tags
•
PCBs
Litsearches
WoS
ToxLine
Remaining
LitSearch August 2015
Toxline
WoS
Home
Learn about HERO
Using HERO
Search HERO
Projects in HERO
Risk Assessment
Transparency & Integrity