Turkey Tail, Yun Zhi · 2018 · Journal Article
High relevanceHeterologous expression of Trametes versicolor laccase in Saccharomyces cerevisiae.
Trametes versicolor
Key points
- Laccase is used in various industrial fields, and it has been the subject of numerous studies
- In this study, we optimized the expression of laccase in Saccharomyces cerevisiae
- Optimizing the culture conditions resulted in an improvement in the expression level, and approximately 45 U/L of laccase was functionally secreted in the culture
- The recombinant laccase was found to be a heavily hypermannosylated glycoprotein, and the molecular weight of the carbohydrate chain was approximately 60 kDa
- These hypermannosylated glycans lowered the substrate affinity, but the optimum pH and thermo-stability were not changed by these hypermannosylated glycans
- This functional expression system described here will aid in molecular evolutionary studies conducted to generate new variants of laccase
Metadata-grounded summary
Citation abstract
Laccase is used in various industrial fields, and it has been the subject of numerous studies. Trametes versicolor laccase has one of the highest redox potentials among the various forms of this enzyme. In this study, we optimized the expression of laccase in Saccharomyces cerevisiae. Optimizing the culture conditions resulted in an improvement in the expression level, and approximately 45 U/L of laccase was functionally secreted in the culture. The recombinant laccase was found to be a heavily hypermannosylated glycoprotein, and the molecular weight of the carbohydrate chain was approximately 60 kDa. These hypermannosylated glycans lowered the substrate affinity, but the optimum pH and thermo-stability were not changed by these hypermannosylated glycans. This functional expression system described here will aid in molecular evolutionary studies conducted to generate new variants of laccase.
Citation
Iimura Y, Sonoki T, Habe H (2018). Heterologous expression of Trametes versicolor laccase in Saccharomyces cerevisiae. Protein expression and purification https://doi.org/10.1016/j.pep.2017.09.004 PMID: 28918197
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