Heterologous Expression and Physicochemical Properties of Plantaricin LPL-1

The present study aimed to express soluble recombinant class Ⅱa bacteriocin in Escherichia coli. The plantaricin LPL-1 gene was cloned into an arabinose promoter, and the C-terminus was fused with the his-tag sequence for expression. The inhibitory activity of recombinant plantaricin LPL-1 against Listeria monocytogenes 54002 was used as the response variable. A novel cell factory, E. coil (ΔtrxB + Δgor + ahpC^M), suitable for class Ⅱa bacteriocin expression was established by CRISPR gene editing technology. It was derived from E. coil BW25331 by deleting the thioredoxin reductase (trxB) gene and glutathione reductase (gor) gene and mutating the gene encoding peroxidase (ahpC). The recombinant plantaricin LPL-1 was purified by affinity chromatography, and its physicochemical properties were analyzed. The purified plantaricin LPL-1 possessed wide pH stability (2–11), high thermal stability (60–100 ℃), and surfactant stability. The recombinant bacteriocin has wide potential for food industrial applications.