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Isolation, Purification, and Characterization of a Laccase-Degrading Aflatoxin B1 from Bacillus amyloliqiens B10
| Content Provider | MDPI |
|---|---|
| Author | Xiong, Dongwei Wen, Jun Lu, Gen Li, Tianxi Long, Miao |
| Copyright Year | 2022 |
| Description | Aflatoxins, widely found in feed and foodstuffs, are potentially harmful to human and animal health because of their high toxicity. In this study, a strain of Bacillus amyloliqiens B10 with a strong ability to degrade aflatoxin B1 (AFB1) was screened; it could degrade 2.5 μg/mL of AFB1 within 96 h. The active substances of Bacillus amyloliqiens B10 for the degradation of AFB1 mainly existed in the culture supernatant. A new laccase with AFB1-degrading activity was separated by ammonium sulfate precipitation, diethylaminoethyl (DEAE) and gel filtration chromatography. The results of molecular docking showed that B10 laccase and aflatoxin had a high docking score. The coding sequence of the laccase was successfully amplified from cDNA by PCR and cloned into E. coli. The purified laccase could degrade 79.3% of AFB1 within 36 h. The optimum temperature for AFB1 degradation was 40 °C, and the optimum pH was 6.0–8.0. Notably, $Mg^{2+}$ and dimethyl sulfoxide (DMSO) could enhance the AFB1-degrading activity of B10 laccase. Mutation of the three key metal combined sites of B10 laccase resulted in the loss of AFB1-degrading activity, indicating that these three metal combined sites of B10 laccase play an essential role in the catalytic degradation of AFB1. |
| Starting Page | 250 |
| e-ISSN | 20726651 |
| DOI | 10.3390/toxins14040250 |
| Journal | Toxins |
| Issue Number | 4 |
| Volume Number | 14 |
| Language | English |
| Publisher | MDPI |
| Publisher Date | 2022-03-31 |
| Access Restriction | Open |
| Subject Keyword | Toxins Aflatoxin Bacillus Amyloliquefaciens Laccase Degradation Molecular Docking Mutagenesis |
| Content Type | Text |
| Resource Type | Article |
