|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|5515971||1400791||2018||5 صفحه PDF||سفارش دهید||دانلود کنید|
- The expression of Trametes versicolor laccase in Saccharomyces cerevisiae was optimized.
- The recombinant laccase was found to be a heavily hypermannosylated glycoprotein.
- The optimum pH and and thermo-stability of the recombinant laccase were not changed.
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 60Â 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.
Journal: Protein Expression and Purification - Volume 141, January 2018, Pages 39-43