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Thermo-Alkali-Tolerant Recombinant Laccase from Bacillus swezeyi and Its Degradation Potential against Zearalenone and Aflatoxin B 1 .
- Source :
-
Journal of agricultural and food chemistry [J Agric Food Chem] 2024 Jun 12; Vol. 72 (23), pp. 13371-13381. Date of Electronic Publication: 2024 May 29. - Publication Year :
- 2024
-
Abstract
- The enzymatic biodegradation of mycotoxins in food and feed has attracted the most interest in recent years. In this paper, the laccase gene from Bacillus swezeyi was cloned and expressed in Escherichia coli BL 21(D3). The sequence analysis indicated that the gene consisted of 1533 bp. The purified B. swezeyi laccase was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis -12% with an estimated molecular weight of 56.7 kDa. The enzyme is thermo-alkali-tolerant, displaying the optimal degradation of zearalenone (ZEN) and aflatoxin B <subscript>1</subscript> (AFB <subscript>1</subscript> ) at pH 8 and 9, with incubation temperatures of 55 and 50 °C, respectively, within 24 h. The degradation potentials of the 50 μg of the enzyme against ZEN (5.0 μg/mL) and AFB <subscript>1</subscript> (2.5 μg/mL) were 99.60 and 96.73%, respectively, within 24 h. To the best of our knowledge, this is the first study revealing the recombinant production of laccase from B. swezeyi , its biochemical properties, and potential use in ZEN and AFB <subscript>1</subscript> degradation in vitro and in vivo.
- Subjects :
- Hydrogen-Ion Concentration
Temperature
Molecular Weight
Escherichia coli genetics
Escherichia coli metabolism
Cloning, Molecular
Alkalies metabolism
Alkalies chemistry
Laccase genetics
Laccase metabolism
Laccase chemistry
Aflatoxin B1 metabolism
Aflatoxin B1 chemistry
Zearalenone metabolism
Zearalenone chemistry
Bacillus enzymology
Bacillus genetics
Bacillus metabolism
Bacterial Proteins genetics
Bacterial Proteins metabolism
Bacterial Proteins chemistry
Enzyme Stability
Recombinant Proteins metabolism
Recombinant Proteins genetics
Recombinant Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1520-5118
- Volume :
- 72
- Issue :
- 23
- Database :
- MEDLINE
- Journal :
- Journal of agricultural and food chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 38809574
- Full Text :
- https://doi.org/10.1021/acs.jafc.4c01304