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a Department of Biochemistry and Molecular Biology, The University of Georgia, Athens, Georgia, USA
Key Words: acetyl xylan esterase • anaerobic fungi • cellulases • cyclophilin • feruloyl and coumaroyl esterases • fungal cellulosomes • glucanase • glucosidase • hemicellulases • herbivorous animals • mannanase • Orpinomyces PC-2 • xylanases
Address for correspondence: Lars G. Ljungdahl, Department of Biochemistry and Molecular Biology, Fred C. Davison Life Sciences Complex, University of Georgia, Athens, GA 30602-7229. Voice: +1-706-542-1334 or +1-706-548-5190; fax: +1-706-542-1738. Larsljd{at}bmb.uga.edu
Anaerobic fungi, first described in 1975 by Orpin, live in close contact with bacteria and other microorganisms in the rumen and caecum of herbivorous animals, where they digest ingested plant food. Seventeen distinct anaerobic fungi belonging to five different genera have been described. They have been found in at least 50 different herbivorous animals. Anaerobic fungi do not possess mitochondria, but instead have hydrogenosomes, which form hydrogen and carbon dioxide from pyruvate and malate during fermentation of carbohydrates. In addition, they are very oxygen- and temperature-sensitive, and their DNA has an unusually high AT content of from 72 to 87 mol%. My initial reason for studying anaerobic fungi was because they solubilize lignocellulose and produce all enzymes needed to efficiently hydrolyze cellulose and hemicelluloses. Although some of these enzymes are found free in the medium, most of them are associated with cellulosomal and polycellulosomal complexes, in which the enzymes are attached through fungal dockerins to scaffolding proteins; this is similar to what has been found for cellulosomes from anaerobic bacteria. Although cellulosomes from anaerobic fungi share many properties with cellulosomes of anaerobic cellulolytic bacteria and have comparable structures, their structures differ in their amino acid sequences. I discuss some features of the cellulosome of the anaerobic fungus Orpinomyces sp. PC-2 and some possible uses of its enzymes in industrial settings.
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