Next Article in Journal
Signal Enhancement of Cadmium in Lettuce Using Laser-Induced Breakdown Spectroscopy Combined with Pyrolysis Process
Previous Article in Journal
Thermal Decomposition of Maya Blue: Extraction of Indigo Thermal Decomposition Steps from a Multistep Heterogeneous Reaction Using a Kinetic Deconvolution Analysis
Previous Article in Special Issue
A Novel Cold-Adapted and Salt-Tolerant RNase R from Antarctic Sea-Ice Bacterium Psychrobacter sp. ANT206
Article Menu
Issue 13 (July-1) cover image

Export Article

Open AccessArticle

Molecular Characterization and Heterologous Production of the Bacteriocin Peocin, a DNA Starvation/Stationary Phase Protection Protein, from Paenibacillus ehimensis NPUST1

1
Department of Dentistry, Zuoying Branch of Kaohsiung Armed Forces General Hospital, Kaohsiung 81357, Taiwan
2
Department of Marine Biotechnology and Resources, National Sun Yat-sen University, Kaohsiung 80424, Taiwan
3
Department of Biological Science and Technology, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan
4
Department of Fisheries and Marine Science, University of Brawijaya, Malang 65145, Indonesia
5
Department of Environmental Biology and Fisheries Science, National Taiwan Ocean University, Keelung 20224, Taiwan
6
Department of Clinical pharmacy, Zuoying Branch of Kaohsiung Armed Forces General Hospital, Kaohsiung 81357, Taiwan
7
Research Center for Animal Biologics, National Pingtung University of Science and Technology, Pingtung 912, Taiwan
*
Authors to whom correspondence should be addressed.
Chung-Chih Tseng and Lini Murni contributed equally to this work.
Academic Editor: Derek J. McPhee
Molecules 2019, 24(13), 2516; https://doi.org/10.3390/molecules24132516
Received: 13 May 2019 / Revised: 2 July 2019 / Accepted: 8 July 2019 / Published: 9 July 2019
(This article belongs to the Special Issue Biotechnology of Microbial Enzymes)
  |  
PDF [2229 KB, uploaded 11 July 2019]
  |     |  

Abstract

The production of a bacteriocin-like substance with antimicrobial activity, named peocin, by the probiotic Paenibacillus ehimensis NPUST1 was previously reported by our laboratory. The present study aimed to identify peocin and increase the peocin yield by heterologous expression in Escherichia coli BL21(DE3). Peocin was identified as a DNA starvation/stationary phase protection protein, also called DNA-binding protein from starved cells (Dps), by gel overlay and LC-MS/MS analysis. For mass production of peocin, fed-batch cultivation of E. coli was performed using a pH-stat control system. Purification by simple nickel affinity chromatography and dialysis yielded 45.3 mg of purified peocin from a 20-mL fed-batch culture (49.3% recovery). The biological activity of the purified peocin was confirmed by determination of the MIC and MBC against diverse pathogens. Purified peocin exhibited antimicrobial activity against aquatic, food spoilage, clinical and antibiotic-resistant pathogens. In an in vivo challenge test, zebrafish treated with purified peocin exhibited significantly increased survival rates after A. hydrophila challenge. The present study is the first to show the antimicrobial activity of Dps and provides an efficient strategy for production of bioactive peocin, which will aid the development of peocin as a novel antimicrobial agent with potential applications in diverse industries. View Full-Text
Keywords: bacteriocin; DNA starvation/stationary phase protection protein; fed-batch culture; Escherichia coli; antimicrobial activity bacteriocin; DNA starvation/stationary phase protection protein; fed-batch culture; Escherichia coli; antimicrobial activity
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Supplementary material

SciFeed

Share & Cite This Article

MDPI and ACS Style

Tseng, C.-C.; Murni, L.; Han, T.-W.; Arfiati, D.; Shih, H.-T.; Hu, S.-Y. Molecular Characterization and Heterologous Production of the Bacteriocin Peocin, a DNA Starvation/Stationary Phase Protection Protein, from Paenibacillus ehimensis NPUST1. Molecules 2019, 24, 2516.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top