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We report here a successful expression of a single-module GH-7 family cellobiohydrolase Cel7A from a thermophilic fungus  Talaromyces emersonii  ( Te  Cel7A) in  Saccharomyces cerevisiae . The heterologous expression system allowed structure-guided protein engineering to improve the thermostability and activity of  Te  Cel7A. Altogether six different mutants aimed at introducing additional disulphide bridges to the catalytic module of  Te  Cel7A were designed. These included addition of five individual S-S bridges in or between the loops extending from the β-sandwich fold, and located either near the active site tunnel or forming the tunnel in  Te  Cel7A. A triple mutant containing the three best S-S mutations was also engineered. Three out of five single S-S mutants all had clearly improved thermostability which was also reflected as improved Avicel hydrolysis efficiency at 75°C. The best mutant was the triple mutant whose unfolding temperature was improved by 9°C leading to efficient microcrystalline cellulose hydrolysis at 80°C. All the additional S-S bonds contributed mainly to the thermostability of the  Te  Cel7A, but one of the mutants (N54C/P191C) also showed, somewhat surprisingly, improved activity even at room temperature.

protein engineering, design and selection

Expression of  Talaromyces emersonii  cellobiohydrolase Cel7A in  Saccharomyces cerevisiae  and rational mutagenesis to improve its thermostability and activity