Journal
TOXINS
Volume 14, Issue 7, Pages -Publisher
MDPI
DOI: 10.3390/toxins14070440
Keywords
patulin; mycotoxin; manganese peroxidase; apple juice; detoxification
Categories
Funding
- National Key R&D Program of China [2021YFA0910602, 2021YFC2103002, 2021YFC2102400]
- National Chicken Industry Technology System of China [CARS-41]
Ask authors/readers for more resources
Patulin, a mycotoxin commonly found in foods and beverages, can be efficiently degraded by a manganese peroxidase enzyme. The enzyme was able to rapidly degrade patulin and detoxify it, making it a potential candidate for enzymatic detoxification in food and beverages.
The fungal secondary metabolite patulin is a mycotoxin widespread in foods and beverages which poses a serious threat to human health. However, no enzyme was known to be able to degrade this mycotoxin. For the first time, we discovered that a manganese peroxidase (MrMnP) from Moniliophthora roreri can efficiently degrade patulin. The MrMnP gene was cloned into pPICZ alpha(A) and then the recombinant plasmid was transformed into Pichia pastoris X-33. The recombinant strain produced extracellular manganese peroxidase with an activity of up to 3659.5 U/L. The manganese peroxidase MrMnP was able to rapidly degrade patulin, with hydroascladiol appearing as a main degradation product. Five mg/L of pure patulin were completely degraded within 5 h. Moreover, up to 95% of the toxin was eliminated in a simulated patulin-contaminated apple juice after 24 h. Using Escherichia coli as a model, it was demonstrated that the deconstruction of patulin led to detoxification. Collectively, these traits make MrMnP an intriguing candidate useful in enzymatic detoxification of patulin in foods and beverages.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available