Thursday April 1


Parallel session 8: Fungal Biotechnology



Fungal biotechnology: lessons learned from Penicillium strain improvement

Roel Bovenberg, Marco van den Berg

DSM Biotechnology Center


Production of penicillin by Penicillium chrysogenum is a classic hallmark of fungal biotechnology. Since its famous discovery by Fleming and initial production during the Second World War penicillin production has increased enormously as a result of strain and process improvements. Using metabolic pathway engineering high yielding penicillin strains were also converted in efficient cephalosporin producers. Recently, we determined the full genome sequence of Penicillium and developed post genomic tools to study the Penicillium strain lineage for mutations acquired in the long optimization process. In addition basic studies on fungal metabolism, microbody formation and transporters have increased our knowledge on penicillin formation significantly. The presentation will cover both basic and applied aspects of the research done.





Fungal enzyme expression as a unit operation in the production of cellulosic ethanol

N. Jamie Ryding

Verenium Corporation


Verenium is a leader in the development of  next-generation cellulosic ethanol as well as the development of Specialty Enzyme Products. Vereniumís cellulosic ethanol process utilizes on-site, fungal enzyme production to supply the enzymes for the saccharification of the cellulose fiber stream in a continuous saccharification-fermentation process.  Fungal enzyme production is a significant unit operation within the facility and successful integration of this unit operation into the overall process presents a number of challenges and opportunities. These experiences will be discussed in the context of the operation of Vereniumís 1.4 MGY demonstration plant in Jennings, LA. In addition, the data obtained from Demonstration Plant operation are helping to guide the development of Vereniumís process-optimized lignocellulosic enzyme cocktail. This high performance fungal enzyme cocktail is anticipated to become a key differentiating component of Vereniumís commercial cellulosic ethanol process.


Genomic and transcriptomic analysis of Thielavia terrestris Ė a thermophilic ascomycete of biotechnological interest

Randy M. Berka[1] Adrian Tsang[2] Robert Otillar[3] Jeremy Schmutz[9] Jane Grimwood[9] Asaf Salamov[9]  Bernard Henrissat[4] Pedro M. Coutinho[4] Vincent Lombard[4] John Clutterbuck[5] Ian Paulsen[6] Scott Baker[7] Jon Magnuson[7] Don Natvig[8] Justin Powlowski[2] Paul Harris[1] Ian Reid[2] Amy Powell[10] Diego Martinez[8] Mark Wogulis[1] Alfredo Lopez de Leon[1] Michael W. Rey[1] and Igor V. Gregoriev[3]

1Novozymes, Inc., 2Concordia University, 3Joint Genome Institute, 4Architecture et Fonction des Macromolecules Biologiques Universite Aix-Marseille, 5University of Glasgow, 6Macquarie University, 7Pacific Northwest National Laboratory, 8University of New Mexico, 9JGI-HudsonAlpha Institute for Biotechnology 10Sandia National Laboratories


Thielavia terrestris (anamorph = Acremonium alabamense) is a thermophilic ascomycete that is of interest as a potential source of thermostable enzymes for biotechnological applications such as biomass decomposition.  A high-quality draft genome sequence of T. terrestris NRRL 8126 was recently completed at the Joint Genome Institute.  Subsequent mining, editing, and annotation efforts are in progress by an international team of collaborators.  The genome assembly comprises eight scaffolds (231 contigs) spanning 36.9 Mbp (sequence coverage = 10.15x).  The overall G+C content, excluding mitochondrial DNA, was approximately 58%.  The presence of telomeric repeats [(TTAGGG)n/(CCCTAA)n] at both ends of scaffolds 1,3, 4 and 6, and at one end of scaffolds 2, 5, 7 and 8 suggests that the assembly contains nearly complete chromosome sequences. Among the 9815 predicted protein-coding genes in the Thielavia genome, >750 transposases were identified on the basis sequence identity with Aspergillus nidulans transposons, and a sizeable proportion of these appear to be degraded by RIP.  Approximately 6-8% of the gene models are predicted to encode secreted proteins such as oxidoreductases, peptidases and a variety of glycoside hydrolases. Compared to the well-studied cellulolytic fungus Trichoderma reesei, an obvious expansion of genes encoding family GH61 proteins was noted.  Nimblegen expression arrays were deployed in a preliminary investigation to compare the transcription profiles of T. terrestris cells grown on several substrates (e.g., glucose, cellulose, xylan, soy flour), and induction of genes predicted to encode cellulases and hemicellulases was observed on cellulose and xylan, respectively.  A comparison of transcriptome data for cells grown in glucose medium at 34įC and 45įC suggested that growth of T. terrestris at the higher temperature may induce expression of genes encoding membrane proteins, sterol biosynthetic enzymes, heat shock proteins/chaperones and components of the ubiquitin proteasome pathway.








return to table of contents