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 498438
Title Protein identification and in vitro digestion of fractions from Tenebrio molitor
Author(s) Yi, Liya; Boekel, M.A.J.S. van; Boeren, Sjef; Lakemond, Catriona M.M.
Source European Food Research and Technology 242 (2016). - ISSN 1438-2377 - p. 1285 - 1297.
DOI https://doi.org/10.1007/s00217-015-2632-6
Department(s) Food Quality and Design
Biochemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2016
Keyword(s) In vitro digestion - Insect protein - LC–MS/MS - Protein identification - Tenebrio molitor
Abstract

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.

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