This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jäger, A.
Right arrow Articles by Kirk, T. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jäger, A.
Right arrow Articles by Kirk, T. K.
Agricola
Right arrow Articles by Jäger, A.
Right arrow Articles by Kirk, T. K.

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1985 November; 50(5): 1274-1278

Production of Ligninases and Degradation of Lignin in Agitated Submerged Cultures of Phanerochaete chrysosporium

Alexander Jäger{dagger}, Suki Croan and T. Kent Kirk*

Forest Products Laboratory, Forest Service, U. S. Department of Agriculture, Madison, Wisconsin 53705

ABSTRACT

Research on the extracellular hemeprotein ligninases of Phanerochaete chrysosporium has been hampered by the necessity to produce them in stationary culture. This investigation examined the effects of detergents on development of ligninase activity in agitated submerged cultures. Results show that addition of Tween 80, Tween 20, or 3-[(3-colamidopropyl)dimethylammonio]1-propanesulfonate to the cultures permits development of ligninase activity comparable to that routinely obtained in stationary cultures. The detergent-amended cultures express the entire ligninolytic system, assayed as the complete oxidation of [14C]lignin to 14CO2. The detergent effect is evidently not merely in facilitating release of extant enzyme. Development of ligninolytic activity in the agitated cultures, as in stationary cultures, is idiophasic. Ion-exchange fast protein-liquid chromatography indicated that the heme protein profiles in agitated and stationary cultures are very similar. These findings should make it possible to scale up production of ligninolytic enzymes in stirred tank fermentors.


FOOTNOTES

* Corresponding author.

{dagger} Present address: Laboratorium fur Technische Biochemie, Universitat Hohenheim, Stuttgart 70, Federal Republic of Germany.


Appl Environ Microbiol. 1985 November; 50(5): 1274-1278




This article has been cited by other articles:

  • Zacchi, L., Morris, I., Harvey, P. J. (2000). Disordered ultrastructure in lignin-peroxidase-secreting hyphae of the white-rot fungus Phanerochaete chrysosporium. Microbiology 146: 759-765 [Abstract] [Full Text]