Protein identification and in vitro digestion of fractions from Tenebrio molitor

Liya Yi*, M.A.J.S. van Boekel, Sjef Boeren, Catriona M.M. Lakemond

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

23 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1285-1297
JournalEuropean Food Research and Technology
Volume242
DOIs
Publication statusPublished - 2016

Fingerprint

Tenebrio
Tenebrio molitor
in vitro digestion
Digestion
Proteins
pellets
proteins
muscle protein
pepsin
digestible protein
amino acid composition
hemolymph
Hemolymph
Muscle Proteins
Pepsin A
digestibility
digestion
insect proteins
pancreatin
Insect Proteins

Keywords

  • In vitro digestion
  • Insect protein
  • LC–MS/MS
  • Protein identification
  • Tenebrio molitor

Cite this

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title = "Protein identification and in vitro digestion of fractions from 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.",
keywords = "In vitro digestion, Insect protein, LC–MS/MS, Protein identification, Tenebrio molitor",
author = "Liya Yi and {van Boekel}, M.A.J.S. and Sjef Boeren and Lakemond, {Catriona M.M.}",
year = "2016",
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language = "English",
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}

Protein identification and in vitro digestion of fractions from Tenebrio molitor. / Yi, Liya; van Boekel, M.A.J.S.; Boeren, Sjef; Lakemond, Catriona M.M.

In: European Food Research and Technology, Vol. 242, 2016, p. 1285-1297.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Protein identification and in vitro digestion of fractions from Tenebrio molitor

AU - Yi, Liya

AU - van Boekel, M.A.J.S.

AU - Boeren, Sjef

AU - Lakemond, Catriona M.M.

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

KW - In vitro digestion

KW - Insect protein

KW - LC–MS/MS

KW - Protein identification

KW - Tenebrio molitor

U2 - 10.1007/s00217-015-2632-6

DO - 10.1007/s00217-015-2632-6

M3 - Article

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JO - European Food Research and Technology

JF - European Food Research and Technology

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ER -