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Article Abstract
Patulin (PAT) is a mycotoxin widely found in fruits, which has various toxicological effects and seriously affects the safety of fruits and related products. Since PAT is stable in nature, developing bio-enzymatic degradation methods has become the predominant focus of current research. This study cloned a potential reductase gene capable of PAT degradation from Wickerhamomyces ciferrii and characterized the recombinant enzyme properties in detail. The recombinant enzyme is not metal ion dependent, and exhibited the highest activity at pH 6.5 and 50 °C for PAT degradation. Notably, the enzyme could degrade a wide range of PAT content from 5 to 40 μg/mL at a low enzyme concentration (25 μg/mL) in the presence of cofactor NADPH. The docking study of the enzyme and PAT as well as the virtual mutagenesis indicated that residues of Ser141, Tyr157 and His186 are significant for the transformation of PAT in the presence of NADPH.
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| http://dx.doi.org/10.1016/j.ijbiomac.2025.145656 | DOI Listing |
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Identification and application of the reductase from Wickerhamomyces ciferrii for the degradation of patulin.
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Article Synopsis
- Ceramides, crucial in skincare and pharmaceuticals, are derived from long-chain fatty acids and phytosphingosine, but sourcing phytosphingosine from plants is difficult due to low concentrations.
- The main method for producing phytosphingosine is through the deacetylation of tetraacetyl phytosphingosine (TAPS), which is primarily obtained from a specific yeast that can naturally secrete TAPS.
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