Isolation and identification of a novel LCI like antibacterial protein from Bacillus sp. MD-5 reveals its potential application in controlling Staphylococcus aureus in food industry

Isolation and identification of a novel LCI like antibacterial protein from Bacillus sp. MD-5... A novel LCI like antibacterial protein produced by Bacillus sp. MD-5, which was isolated from the Arctic Ocean sediment sample during the sixth Chinese National Arctic Expedition in 2014, was purified and characterized. After saturation of Bacillus sp. MD-5 culture supernatant with ammonium sulfate and separation with ion-exchange chromatography and high performance liquid chromatography (HPLC), an antibacterial protein (MD) was purified. The MD protein was determined to be a novel LCI like antibacterial protein with molecular weight of about 7.0 kDa using liquid chromatograph-mass spectrometer (LC-MS) identification and the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). It displayed antibacterial activity against Staphylococcus aureus at minimum inhibitory concentration (MIC) of 7.33 μg/mL. MD protein possessed high thermostability and wide range of pH tolerance, and had a certain extent of protease, surfactant and metal ion resistance. MD protein was suggested to inhibit the growth of S. aureus through inhibiting peptidoglycan biosynthesis in the view of TEM detection. These results suggested that MD may represent a novel antibacterial protein with potential application in controlling S. aureus in food industry. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Food Control Elsevier

Isolation and identification of a novel LCI like antibacterial protein from Bacillus sp. MD-5 reveals its potential application in controlling Staphylococcus aureus in food industry

Loading next page...
 
/lp/elsevier/isolation-and-identification-of-a-novel-lci-like-antibacterial-protein-v7mv0NUrNt
Publisher
Elsevier
Copyright
Copyright © 2018 Elsevier Ltd
ISSN
0956-7135
eISSN
1873-7129
D.O.I.
10.1016/j.foodcont.2018.01.026
Publisher site
See Article on Publisher Site

Abstract

A novel LCI like antibacterial protein produced by Bacillus sp. MD-5, which was isolated from the Arctic Ocean sediment sample during the sixth Chinese National Arctic Expedition in 2014, was purified and characterized. After saturation of Bacillus sp. MD-5 culture supernatant with ammonium sulfate and separation with ion-exchange chromatography and high performance liquid chromatography (HPLC), an antibacterial protein (MD) was purified. The MD protein was determined to be a novel LCI like antibacterial protein with molecular weight of about 7.0 kDa using liquid chromatograph-mass spectrometer (LC-MS) identification and the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). It displayed antibacterial activity against Staphylococcus aureus at minimum inhibitory concentration (MIC) of 7.33 μg/mL. MD protein possessed high thermostability and wide range of pH tolerance, and had a certain extent of protease, surfactant and metal ion resistance. MD protein was suggested to inhibit the growth of S. aureus through inhibiting peptidoglycan biosynthesis in the view of TEM detection. These results suggested that MD may represent a novel antibacterial protein with potential application in controlling S. aureus in food industry.

Journal

Food ControlElsevier

Published: Jul 1, 2018

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 12 million articles from more than
10,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Unlimited reading

Read as many articles as you need. Full articles with original layout, charts and figures. Read online, from anywhere.

Stay up to date

Keep up with your field with Personalized Recommendations and Follow Journals to get automatic updates.

Organize your research

It’s easy to organize your research with our built-in tools.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve Freelancer

DeepDyve Pro

Price
FREE
$49/month

$360/year
Save searches from
Google Scholar,
PubMed
Create lists to
organize your research
Export lists, citations
Read DeepDyve articles
Abstract access only
Unlimited access to over
18 million full-text articles
Print
20 pages/month
PDF Discount
20% off