Next Article in Journal
Understanding the Snake Venom Metalloproteinases: An Interview with Jay Fox and José María Gutiérrez
Next Article in Special Issue
Patulin Degradation by the Biocontrol Yeast Sporobolomyces sp. Is an Inducible Process
Previous Article in Journal
The Influence of the Toxin/Antitoxin mazEF on Growth and Survival of Listeria monocytogenes under Stress
Previous Article in Special Issue
Degradation of Aflatoxins by Means of Laccases from Trametes versicolor: An In Silico Insight
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessArticle
Toxins 2017, 9(1), 36; doi:10.3390/toxins9010036

Novel Aflatoxin-Degrading Enzyme from Bacillus shackletonii L7

1
Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, 1 Nongda South Road, Xibeiwang Town, Haidian District, Beijing 100193, China
2
Key Laboratory of Agro-products Processing, Ministry of Agriculture, 1 Nongda South Road, Xibeiwang Town, Haidian District, Beijing 100193, China
3
Shenyang Institute of Engineering, No.18 Puchang Road, Shenbei New District, Shenyang 110136, China
These authors contributed equally to this work.
Presently address: College of Life Sciences, Hubei University, Wuhan 430062, China.
*
Author to whom correspondence should be addressed.
Academic Editor: Ting Zhou
Received: 22 September 2016 / Revised: 10 January 2017 / Accepted: 11 January 2017 / Published: 14 January 2017
View Full-Text   |   Download PDF [3161 KB, uploaded 14 January 2017]   |  

Abstract

Food and feed contamination by aflatoxin (AF)B1 has adverse economic and health consequences. AFB1 degradation by microorganisms or microbial enzymes provides a promising preventive measure. To this end, the present study tested 43 bacterial isolates collected from maize, rice, and soil samples for AFB1-reducing activity. The higher activity was detected in isolate L7, which was identified as Bacillus shackletonii. L7 reduced AFB1, AFB2, and AFM1 levels by 92.1%, 84.1%, and 90.4%, respectively, after 72 h at 37 °C. The L7 culture supernatant degraded more AFB1 than viable cells and cell extracts; and the degradation activity was reduced from 77.9% to 15.3% in the presence of proteinase K and sodium dodecyl sulphate. A thermostable enzyme purified from the boiled supernatant was designated as Bacillus aflatoxin-degrading enzyme (BADE). An overall 9.55-fold purification of BADE with a recovery of 39.92% and an activity of 3.85 × 103 U·mg−1 was obtained using chromatography on DEAE-Sepharose. BADE had an estimated molecular mass of 22 kDa and exhibited the highest activity at 70 °C and pH 8.0, which was enhanced by Cu2+ and inhibited by Zn2+, Mn2+, Mg2+, and Li+. BADE is the major protein involved in AFB1 detoxification. This is the first report of a BADE isolated from B. shackletonii, which has potential applications in the detoxification of aflatoxins during food and feed processing. View Full-Text
Keywords: aflatoxin B1; aflatoxin-degrading enzyme; biodegradation; Bacillus shackletonii; purification aflatoxin B1; aflatoxin-degrading enzyme; biodegradation; Bacillus shackletonii; purification
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 alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Xu, L.; Eisa Ahmed, M.F.; Sangare, L.; Zhao, Y.; Selvaraj, J.N.; Xing, F.; Wang, Y.; Yang, H.; Liu, Y. Novel Aflatoxin-Degrading Enzyme from Bacillus shackletonii L7. Toxins 2017, 9, 36.

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]
Toxins EISSN 2072-6651 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top