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 547698
Title Effect of endogenous phenoloxidase on protein solubility and digestibility after processing of Tenebrio molitor, Alphitobius diaperinus and Hermetia illucens
Author(s) Janssen, Renske H.; Vincken, Jean Paul; Arts, Nathalie J.G.; Fogliano, Vincenzo; Lakemond, Catriona M.M.
Source Food Research International 121 (2019). - ISSN 0963-9969 - p. 684 - 690.
DOI https://doi.org/10.1016/j.foodres.2018.12.038
Department(s) Food Chemistry
Food Quality and Design
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2019
Keyword(s) Black soldier fly - Digestion - Edible insects - Enzymatic browning - Lesser mealworm - Phenoloxidase - Protease - Protein extraction - Solubility - Tyrosinase - Yellow mealworm
Abstract

Upon extracting soluble proteins from insects as potential food ingredient, endogenous enzymes, such as phenoloxidases, are expected to negatively affect protein properties. The effect of phenoloxidases on solubility and digestibility of proteins was investigated for larvae of Tenebrio molitor, Alphitobius diaperinus and Hermetia illucens. Phenoloxidase inhibition was done using blanching (50 s, 90 °C) before extraction or extracting in presence of sulfite. Similar soluble protein yields and compositions were found without and with sulfite addition, whereas blanching decreased soluble protein yield. Upon in-vitro hydrolysis by pepsin and trypsin, soluble proteins from H. illucens were more digestible than those of T. molitor and A. diaperinus. Phenoloxidase activity during grinding negatively affected in-vitro pepsin hydrolysis. Besides phenoloxidase activity, also endogenous proteases were shown to remain active at pH 8 in extracts containing sulfite and after blanching of larvae. This stresses that protease activity needs to be carefully controlled in the design of insect based ingredients.

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