Effect of endogenous phenoloxidase on protein solubility and digestibility after processing of Tenebrio molitor, Alphitobius diaperinus and Hermetia illucens

Renske H. Janssen, Jean Paul Vincken, Nathalie J.G. Arts, Vincenzo Fogliano, Catriona M.M. Lakemond

Research output: Contribution to journalArticleAcademicpeer-review

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.

Original languageEnglish
Pages (from-to)684-690
Number of pages7
JournalFood Research International
Volume121
Early online date24 Dec 2018
DOIs
Publication statusPublished - Jul 2019

Fingerprint

Hermetia illucens
Alphitobius diaperinus
Tenebrio
Tenebrio molitor
Monophenol Monooxygenase
protein solubility
monophenol monooxygenase
digestible protein
Solubility
Sulfites
blanching
sulfites
Pepsin A
pepsin
Proteins
proteins
Larva
Hydrolysis
Peptide Hydrolases
ingredients

Keywords

  • Black soldier fly
  • Digestion
  • Edible insects
  • Enzymatic browning
  • Lesser mealworm
  • Phenoloxidase
  • Protease
  • Protein extraction
  • Solubility
  • Tyrosinase
  • Yellow mealworm

Cite this

@article{c0fa75dca280401ea0971137f6b16911,
title = "Effect of endogenous phenoloxidase on protein solubility and digestibility after processing of Tenebrio molitor, Alphitobius diaperinus and Hermetia illucens",
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.",
keywords = "Black soldier fly, Digestion, Edible insects, Enzymatic browning, Lesser mealworm, Phenoloxidase, Protease, Protein extraction, Solubility, Tyrosinase, Yellow mealworm",
author = "Janssen, {Renske H.} and Vincken, {Jean Paul} and Arts, {Nathalie J.G.} and Vincenzo Fogliano and Lakemond, {Catriona M.M.}",
year = "2019",
month = "7",
doi = "10.1016/j.foodres.2018.12.038",
language = "English",
volume = "121",
pages = "684--690",
journal = "Food Research International",
issn = "0963-9969",
publisher = "Elsevier",

}

TY - JOUR

T1 - Effect of endogenous phenoloxidase on protein solubility and digestibility after processing of Tenebrio molitor, Alphitobius diaperinus and Hermetia illucens

AU - Janssen, Renske H.

AU - Vincken, Jean Paul

AU - Arts, Nathalie J.G.

AU - Fogliano, Vincenzo

AU - Lakemond, Catriona M.M.

PY - 2019/7

Y1 - 2019/7

N2 - 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.

AB - 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.

KW - Black soldier fly

KW - Digestion

KW - Edible insects

KW - Enzymatic browning

KW - Lesser mealworm

KW - Phenoloxidase

KW - Protease

KW - Protein extraction

KW - Solubility

KW - Tyrosinase

KW - Yellow mealworm

U2 - 10.1016/j.foodres.2018.12.038

DO - 10.1016/j.foodres.2018.12.038

M3 - Article

VL - 121

SP - 684

EP - 690

JO - Food Research International

JF - Food Research International

SN - 0963-9969

ER -