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Updated: Feb 10, 2026

Agar-Block Microcosms for Controlled Plant Tissue Decomposition by Aerobic Fungi
Published on: February 3, 2011
Saccharification efficiencies of multi-enzyme complexes produced by aerobic fungi
Ajay Badhan1, Jiangli Huang2, Yuxi Wang1
1Agriculture and Agri-Food Canada, Lethbridge Research Centre, Lethbridge, Alberta, Canada.
Abstract:
In the present study, we have characterized high molecular weight multi-enzyme complexes in two commercial enzymes produced by Trichoderma reesei (Spezyme CP) and Penicillium funiculosum (Accellerase XC). We successfully identified 146-1000 kDa complexes using Blue native polyacrylamide gel electrophoresis (BN-PAGE) to fractionate the protein profile in both preparations. Identified complexes dissociated into lower molecular weight constituents when loaded on SDS PAGE. Unfolding of the secondary structure of multi-enzyme complexes with trimethylamine (pH >10) suggested that they were not a result of unspecific protein aggregation. Cellulase (CMCase) profiles of extracts of BN-PAGE fractionated protein bands confirmed cellulase activity within the multi-enzyme complexes. A microassay was used to identify protein bands that promoted high levels of glucose release from barley straw. Those with high saccharification yield were subjected to LC-MS analysis to identify the principal enzymatic activities responsible. The results suggest that secretion of proteins by aerobic fungi leads to the formation of high molecular weight multi-enzyme complexes that display activity against carboxymethyl cellulose and barley straw.
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