This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by McSweeney, C S Articles by Lowry, J B Search for Related Content PubMed PubMed Citation Articles by McSweeney, C S Articles by Lowry, J B Agricola Articles by McSweeney, C S Articles by Lowry, J B

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1994 August; 60(8): 2985-2989

Solubilization of lignin by the ruminal anaerobic fungus Neocallimastix patriciarum.

Long Pocket Laboratories, CSIRO Division of Tropical Animal Production, Indooroopilly, Queensland, Australia.

ABSTRACT

The ability of the ruminal anaerobic phycomycete Neocallimastix patriciarum to digest model lignin compounds and lignified structures in plant material was studied in batch culture. The fungus did not degrade or transform model lignin compounds that were representative of the predominant intermonomer linkages in lignin, nor did it solubilize acid detergent lignin that had been isolated from spear grass. In a stem fraction of sorghum, 33.6% of lignin was apparently solubilized by the fungus. Solubilization of ester- and either-linked phenolics accounted for 9.2% of the lignin released. The amounts of free phenolic acids detected in culture fluid were equivalent to the apparent loss of ester-linked phenolics from the sorghum substrate. However, the fungus was unable to cleave the ether bond in hydroxycinnamic acid bridges that cross-link lignin and polysaccharide. It is suggested that the majority of the solubilized lignin fraction was a lignin carbohydrate complex containing ether-linked hydroxycinnamic acids. The lignin carbohydrate complex was probably solubilized through dissolution of xylan in the lignin-xylan matrix rather than by lignin depolymerization.

This article has been cited by other articles:

• Blum, D. L., Kataeva, I. A., Li, X.-L., Ljungdahl, L. G. (2000). Feruloyl Esterase Activity of the Clostridium thermocellum Cellulosome Can Be Attributed to Previously Unknown Domains of XynY and XynZ. J. Bacteriol. 182: 1346-1351 [Abstract] [Full Text]