Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 554548
Title Aflatoxin B1 Conversion by Black Soldier Fly (Hermetia illucens) Larval Enzyme Extracts
Author(s) Meijer, Nathan; Stoopen, Geert; Fels-Klerx, H.J. van der; Loon, Joop J.A. van; Carney, John; Bosch, Guido
Source Toxins 11 (2019)9. - ISSN 2072-6651
DOI https://doi.org/10.3390/toxins11090532
Department(s) BU Toxicology, Novel Foods & Agrochains
EPS
Laboratory of Entomology
WIAS
Animal Nutrition
Publication type Refereed Article in a scientific journal
Publication year 2019
Keyword(s) aflatoxin - black soldier fly - BSFL - cytochrome P450 - enzyme induction - Hermetia illucens - metabolic conversion - mycotoxin - S9 fraction
Abstract

The larvae of the black soldier fly (Hermetia illucens L., BSFL) have received increased industrial interest as a novel protein source for food and feed. Previous research has found that insects, including BSFL, are capable of metabolically converting aflatoxin B1 (AFB1), but recovery of total AFB1 is less than 20% when accounting for its conversion to most known metabolites. The aim of this study was to examine the conversion of AFB1 by S9 extracts of BSFL reared on substrates with or without AFB1. Liver S9 of Aroclor-induced rats was used as a reference. To investigate whether cytochrome P450 enzymes are involved in the conversion of AFB1, the inhibitor piperonyl butoxide (PBO) was tested in a number of treatments. The results showed that approximately 60% of AFB1 was converted to aflatoxicol and aflatoxin P1. The remaining 40% of AFB1 was not converted. Cytochrome P450s were indeed responsible for metabolic conversion of AFB1 into AFP1, and a cytoplasmic reductase was most likely responsible for conversion of AFB1 into aflatoxicol.

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