Cutinase is an extracellular esterase with potential industrial applications. When the cutinase from T. fusca was extracellularly expressed in E.coli through an attached pelB signal peptide, 40% of the total enzyme activity was observed in the cell debris although there is no typical membrane-bound area within the protein sequence. Further in vitro experiments showed that only a small fraction of the activity can be extracted when the debris was treated by surfactants, salts or adjusting pH. More interestingly, when the enzyme was expressed without any signal peptide, almost all of the activity was found in the culture media, which was 2.1-fold higher than that of pelB-mediated expression. These unusual phenomena is probably related to the hydrophobic surface property of the cutinase as well as its capability to weakly hydrolyze membrane phospholipids. The underlying molecular mechanism will be further discussed.

Recombinant Thermobifida fusca cutinase exhibits a unique expression pattern in <i>E. coli</i>

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Recombinant Thermobifida fusca cutinase exhibits a unique expression pattern in E. coli