1B-01

 

Fungal Systems for the Expression of Recombinant Enzymes from Thermophilic Microorganisms

 

 

P. L. Bergquist,1,2  V. S. J. Te’o,1 N. C. Curach,1 M. D. Gibbs1 and K. M. H. Nevalainen1

 

 

1Department of Biological Sciences

Biotechnology Research Institute

Macquarie University

North Ryde, Sydney NSW 2109, Australia

Phone:  +61 2 9850 8614

Fax:  +61 2 9850 9748

Email:  peter.bergquist@mq.edu.au

 

2Department of Molecular Medicine & Pathology

University of Auckland Medical School

Auckland, New Zealand

 

 

 

 

 

An efficient expression system is the key for the economically viable bulk production of enzymes for industrial processes.  Expression vectors for Kluyveromyces lactis utilise 2m-like plasmid pKD1 replicon and the K. lactis LAC4 promoter.  Recombinant proteins in Trichoderma reesei are expressed under the strong cellobiohydrolase 1 (cbh1) promoter as a fusion to the secretion signal or the mature CBHI protein sequences.  We have also reconstructed some of the thermophile genes according to fungal codon preferences and demonstrated a dramatic increase in protein production.  We have examined the effect of the expression host on the form and activity of the heterologous Dictyoglomus thermophilum xylanase, XynB, produced in different Trichoderma strains.  XynB was produced in multiple forms in these hosts, the pattern depending on whether all of the potential N-linked glycosylation sites were left intact or removed.  A proteomics approach has been undertaken to identify powerfully expressed proteins produced by T. reesei in order to identify condition-specific promoters.  One of these proteins is HEX1, the major protein of the fungal Woronin body that is predominant under both cellulase-inducing and repressing conditions.  The hex1 gene promoter and terminator sequences have been isolated to make an expression cassette.  The promoter function has been studied in relation to cultivation time and medium composition and appears promising because of its early onset and extensive production of mRNA.