Fate of enniatins and deoxynivalenol during pasta cooking
Nijs, Monique de; Top, Hester van den; Stoppelaar, Joyce de; Lopez Sanchez, Patricia ; Mol, Hans - \ 2016
Food Chemistry 213 (2016). - ISSN 0308-8146 - p. 763 - 767.
Deoxynivalenol - Enniatins - Fate of mycotoxins - LC–MS/MS - Mycotoxins - Pasta - Processing
The fate of deoxynivalenol and enniatins was studied during cooking of commercially available dry pasta in the Netherlands in 2014. Five samples containing relatively high levels of deoxynivalenol and/or enniatins were selected for the cooking experiment. Cooking was performed in duplicate on different days, under standardised conditions, simulating house-hold preparation. Samples were extracted with a mixture of acetonitrile/water followed by salt-induced partitioning. The extracts were analysed by LC–MS/MS. The method limits of detection were 8 μg/kg for deoxynivalenol, 10 μg/kg for enniatin A1 and 5 μg/kg for enniatins A, B and B1. During the cooking of the five dry pasta samples, 60% of the deoxynivalenol and 83–100% of the enniatins were retained in the cooked pasta. It is recommended to study food processing fate of mycotoxins through naturally contaminated materials (incurred materials).
Protein identification and in vitro digestion of fractions from Tenebrio molitor
Yi, Liya ; Boekel, M.A.J.S. van; Boeren, Sjef ; Lakemond, Catriona M.M. - \ 2016
European Food Research and Technology 242 (2016). - ISSN 1438-2377 - p. 1285 - 1297.
In vitro digestion - Insect protein - LC–MS/MS - Protein identification - Tenebrio molitor
The nutritional value of insect protein is evaluated not only in amino acid composition, but also in protein digestibility. The general amino acid composition of Tenebrio molitor has been reported before, but limited knowledge is available on its digestibility. The objective of this study was to investigate in vitro protein digestibility of whole T. molitor larvae, a water-soluble fraction (supernatant) and water-insoluble fractions (pellet and residue), and to identify which proteins were present in the fractions studied. The digestibility of the supernatant fraction (~80 %) was much higher than that of pellet (~50 %) and residue (~24 %) after in vitro gastroduodenal digestion as was determined using the o-phthaldialdehyde (OPA) method. More proteins were digested after pepsin/pancreatin digestion than after only pepsin digestion. The most abundant proteins in the supernatant were hemolymph protein (~12 kDa), alpha-amylase (~50 kDa, a putative allergen), and muscle proteins (e.g. actin 30–50 kDa) in the pellet fraction as determined from LC–MS/MS and SDS-PAGE. In conclusion, the proteins in the soluble fraction that contained hemolymph proteins were more easily digestible than the insoluble, muscle protein-containing fractions.