Excretory expression of IsPETase in E. coli by an enhancer of signal peptides and enhanced PET hydrolysis.

The PET hydrolase from Ideonella sakaiensis (IsPETase) is efficient for PET degradation, which provides a promising solution for environmental contamination by plastics. This study focuses on improving the excretion of IsPETase from E. coli by signal peptide (SP) engineering.

Excretory overexpression of hydrophobins as multifunctional biosurfactants in E. coli.

Hydrophobins are small amphipathic proteins excreted from filamentous fungi that self-assemble into the amphipathic film at hydrophobic/hydrophilic interfaces and can be used in a wide range of biotechnological application such as antimicrobial coatings, biosensors, and drug delivery. Here we describe a simple method for producing functionally active class I and class II hydrophobins in E. coli.

Elucidation of lid open and orientation of lipase activated in interfacial activation by amphiphilic environment.

Lipases have wide applications using as biocatalyst in numerous biotechnological and bioengineering fields, especially function at hydrophobic or amphiphilic interface. Previously, the lipase from Burkholderia ambifaria YCJ01 was significantly activated when immobilized on the amphiphilic environment. In this work, insights into the functional effect of amphiphilic surface on lipase activation are presented by molecular dynamic simulations.

A novel Ffu fusion system for secretory expression of heterologous proteins in Escherichia coli.

Background: The high level of excretion and rapid folding ability of β-fructofuranosidase (β-FFase) in Escherichia coli has suggested that β-FFase from Arthrobacter arilaitensis NJEM01 can be developed as a fusion partner.

Methods: Based on the modified Wilkinson and Harrison algorithm and the preliminary verification of the solubility-enhancing ability of β-FFase truncations, three β-FFase truncations (i.e.