Details
| Original language | English |
|---|---|
| Article number | 6330 |
| Number of pages | 12 |
| Journal | Scientific reports |
| Volume | 15 |
| Issue number | 1 |
| Publication status | Published - 21 Feb 2025 |
Abstract
Aflatoxin B1 (AFB1) is a highly potent mycotoxin that poses a serious threat to human and animal health. This study investigated the biodegradation of AFB1 by the supernatant of submerged cultured Trametes hirsuta, with a focus on identifying and characterizing the responsible enzyme(s). The extracellular enzymes of the white-rot mushroom were extracted from the supernatant and pre-separated using anion exchange fast protein liquid chromatography (FPLC). To pinpoint the specific enzyme, the eluted protein fractions exhibiting the highest degradation activity were subjected to detailed biochemical and proteomic analyses. A second purification step, ultrafiltration, yielded an electrophoretically pure enzyme. Sequencing of tryptic peptides using a nano-LC system coupled to a qQTOF mass spectrometer identified the enzyme as a lignolytic phenoloxidase. The enzyme exhibited a molecular mass of 55.6 kDa and achieved an impressive AFB1 degradation rate of 77.9% under optimized experimental conditions. This is the first fungal lignolytic phenoloxidase capable of aflatoxin degradation without requiring hydrogen peroxide as a cofactor, highlighting its unique catalytic mechanism. It may be used in mycotoxin remediation strategies, such as treating the surfaces of contaminated fruits, vegetables, and nuts.
Keywords
- Aflatoxin B, Biodegradation, Enzyme purification, Phenoloxidase, Trametes hirsuta
ASJC Scopus subject areas
Sustainable Development Goals
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In: Scientific reports, Vol. 15, No. 1, 6330, 21.02.2025.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Aflatoxin B1 (AFB1) biodegradation by a lignolytic phenoloxidase of Trametes hirsuta
AU - Söylemez, Tuncay
AU - Berger, Ralf Günter
AU - Krings, Ulrich
AU - Yamaç, Mustafa
N1 - Publisher Copyright: © The Author(s) 2025.
PY - 2025/2/21
Y1 - 2025/2/21
N2 - Aflatoxin B1 (AFB1) is a highly potent mycotoxin that poses a serious threat to human and animal health. This study investigated the biodegradation of AFB1 by the supernatant of submerged cultured Trametes hirsuta, with a focus on identifying and characterizing the responsible enzyme(s). The extracellular enzymes of the white-rot mushroom were extracted from the supernatant and pre-separated using anion exchange fast protein liquid chromatography (FPLC). To pinpoint the specific enzyme, the eluted protein fractions exhibiting the highest degradation activity were subjected to detailed biochemical and proteomic analyses. A second purification step, ultrafiltration, yielded an electrophoretically pure enzyme. Sequencing of tryptic peptides using a nano-LC system coupled to a qQTOF mass spectrometer identified the enzyme as a lignolytic phenoloxidase. The enzyme exhibited a molecular mass of 55.6 kDa and achieved an impressive AFB1 degradation rate of 77.9% under optimized experimental conditions. This is the first fungal lignolytic phenoloxidase capable of aflatoxin degradation without requiring hydrogen peroxide as a cofactor, highlighting its unique catalytic mechanism. It may be used in mycotoxin remediation strategies, such as treating the surfaces of contaminated fruits, vegetables, and nuts.
AB - Aflatoxin B1 (AFB1) is a highly potent mycotoxin that poses a serious threat to human and animal health. This study investigated the biodegradation of AFB1 by the supernatant of submerged cultured Trametes hirsuta, with a focus on identifying and characterizing the responsible enzyme(s). The extracellular enzymes of the white-rot mushroom were extracted from the supernatant and pre-separated using anion exchange fast protein liquid chromatography (FPLC). To pinpoint the specific enzyme, the eluted protein fractions exhibiting the highest degradation activity were subjected to detailed biochemical and proteomic analyses. A second purification step, ultrafiltration, yielded an electrophoretically pure enzyme. Sequencing of tryptic peptides using a nano-LC system coupled to a qQTOF mass spectrometer identified the enzyme as a lignolytic phenoloxidase. The enzyme exhibited a molecular mass of 55.6 kDa and achieved an impressive AFB1 degradation rate of 77.9% under optimized experimental conditions. This is the first fungal lignolytic phenoloxidase capable of aflatoxin degradation without requiring hydrogen peroxide as a cofactor, highlighting its unique catalytic mechanism. It may be used in mycotoxin remediation strategies, such as treating the surfaces of contaminated fruits, vegetables, and nuts.
KW - Aflatoxin B
KW - Biodegradation
KW - Enzyme purification
KW - Phenoloxidase
KW - Trametes hirsuta
UR - http://www.scopus.com/inward/record.url?scp=85218705420&partnerID=8YFLogxK
U2 - 10.1038/s41598-025-90711-y
DO - 10.1038/s41598-025-90711-y
M3 - Article
AN - SCOPUS:85218705420
VL - 15
JO - Scientific reports
JF - Scientific reports
SN - 2045-2322
IS - 1
M1 - 6330
ER -