Heterologous Expression of Biopreservative Bacteriocins With a View to Low Cost Production

Beatriz Mesa-Pereira,Mary C Rea,Colin Hill,R Paul Ross,Paul D Cotter

doi:10.3389/fmicb.2018.01654

Abstract

Bacteriocins, a heterogenous group of antibacterial ribosomally synthesized peptides, have potential as bio-preservatives in in a wide range of foods and as future therapeutics for the inhibition of antibiotic-resistant bacteria. While many bacteriocins have been characterized, several factors limit their production in large quantities, a requirement to make them commercially viable for food or pharma applications. The identification of new bacteriocins by database mining has been promising, but their potential is difficult to evaluate in the absence of suitable expression systems. E. coli has been used as a heterologous host to produce recombinant proteins for decades and has an extensive set of expression vectors and strains available. Here, we review the different expression systems for bacteriocin production using this host and identify the most important features to guarantee successful production of a range of bacteriocins.

Highlights

Bacteriocins are antimicrobial peptides produced by Gram-negative and Gram-positive bacteria
Only nisin (e.g., Nisaplin R ) and pediocin PA-1 (e.g., ALTA R -2431) have been commercialized to any significant extent and these mainly as food biopreservatives. This may be explained by the multitude of studies that are required before a bacteriocin can be considered commercially viable, including characterization, potent antimicrobial activity, product stability, mechanism of action, mode of delivery, toxicity and assessment of their applications and industrial-scale production (Ingham and Moore, 2007)
In order to provide a guide for a design of a successful expression system for bacteriocin production in this host, the present review focuses on the different systems currently available for bacteriocin production in E. coli

Summary

INTRODUCTION

Bacteriocins are antimicrobial peptides produced by Gram-negative and Gram-positive bacteria. Given these limitations E. coli, the most commonly used organism for heterologous protein production, is an attractive option for the heterologous bacteriocin expression due to its rapid growth on inexpensive media, its extensive genetic characterization and the availability of versatile cloning tools, expression systems and strains (Mergulhao et al, 2004; Rosano and Ceccarelli, 2014; Jia and Jeon, 2016) This could facilitate the functional characterization and establishment of a production process in bacteriocins from sources that are difficult to cultivate, in addition to those bacteriocins discovered by data mining from sequenced bacterial genomes (Kuo et al, 2013), increasing their potential for manufacture and commerialization by food and pharmaceutical industries (Ongey and Neubauer, 2016). The MCS can provide fusion tags to facilitate the purification of the TABLE 1 | Bacteriocins heterologously produced by E. coli

COLI STRAINS FOR BACTERIOCIN EXPRESSION

CONCLUSION