Enhanced Extracellular Production of <i>Is</i>PETase in <i>Escherichia coli</i> via Engineering of the pelB Signal Peptide
Lixia Shi, Haifeng Liu, Songfeng Gao, Yunxuan Weng, Leilei Zhu
Abstract
BL21 using a Sec-dependent translocation signal peptide, pelB, for secretion. Furthermore, engineering of the pelB through random mutagenesis and screening was performed to improve the secretion efficiency of PETase. Evolved pelB enabled higher PETase secretion by up to 1.7-fold. The improved secretion of PETase led to more efficient hydrolysis of the PET model compound, bis (2-hydroxyethyl) terephthalic acid (BHET), PET powder, and PET film. Our study presents the first example of the increasing secretion of PETase by an engineered signal peptide, providing a promising approach to obtain extracellular PETase for efficient enzymatic degradation of PET.
Topics & Concepts
Escherichia coliSecretionChemistryExtracellularTerephthalic acidSignal peptideHydrolysisEnzymePeptideBiocompatibilityBiochemistryOrganic chemistryRecombinant DNAPolyesterGeneMicroplastics and Plastic PollutionGraphene and Nanomaterials Applicationsbiodegradable polymer synthesis and properties