Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase-IV inhibitors

Irene Dávalos Terán, Kento Imai, Isabelle M.E. Lacroix, Vincenzo Fogliano, Chibuike C. Udenigwe*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Bioinformatics was applied for strategic processing of yellow mealworm (Tenebrio molitor) proteins to produce dipeptidyl peptidase (DPP)-IV inhibiting peptides. In silico analysis of 384 mealworm proteins revealed structural proteins as better precursors of DPP-IV inhibiting peptides, compared with other protein types, after pepsin and papain hydrolysis. This was associated with the higher hydropathicity and amounts of residues associated with DPP-IV inhibition in the structural (cuticular) proteins. In silico, the peptides were mostly released with pepsin than papain. Cuticular (CP) and non-cuticular proteins (NC) were extracted from yellow mealworm and hydrolyzed with pepsin and papain in vitro to validate the virtual findings. CP hydrolysate with papain inhibited DPP-IV the most compared to CP hydrolysate with pepsin, whereas NC hydrolysates were mostly inactive. CP had higher hydrophobic–hydrophilic amino acid ratios and contents of the activity-associated residues than NC. The findings demonstrate the application of bioinformatics in processing proteins for bioactive peptide production. Practical applications: The discovery of bioactive peptides from food proteins is typically based on the classic approach involving working with a small number of protein-protease combinations in vitro. For the first time, this study reported the application of in silico tools in comprehensively studying hundreds of proteins from yellow mealworm (an edible insect) as sources of DPP-IV inhibitors, followed by in vitro processing and validation guided by the results obtained in silico. The advantage of this approach is that it allows for analysis of several protein–protease combinations (with multiple datasets of structural, functional, and bioactivity parameters) in a short time. This work is relevant in advancing research on emerging or alternative proteins as well as structure-informed food protein processing. The bioinformatics approach can be adapted for strategic processing of proteins in the food industry prior to making major resource investments.

Original languageEnglish
Article numbere13121
JournalJournal of food biochemistry
DOIs
Publication statusE-pub ahead of print - 28 Nov 2019

Fingerprint

Tenebrio
Dipeptidyl-Peptidase IV Inhibitors
Tenebrio molitor
Proteome
proteome
Computational Biology
bioinformatics
papain
pepsin
Proteins
peptides
proteins
Dipeptidyl Peptidase 4
Papain
Pepsin A
protein sources
Computer Simulation
hydrolysates
Peptides
edible insects

Keywords

  • bioactive peptides
  • bioinformatics
  • cuticular proteins
  • dipeptidyl peptidase-IV
  • edible insects
  • hydrophobicity
  • Tenebrio molitor

Cite this

@article{b8c0e5569a814f0abe23b0818e502973,
title = "Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase-IV inhibitors",
abstract = "Bioinformatics was applied for strategic processing of yellow mealworm (Tenebrio molitor) proteins to produce dipeptidyl peptidase (DPP)-IV inhibiting peptides. In silico analysis of 384 mealworm proteins revealed structural proteins as better precursors of DPP-IV inhibiting peptides, compared with other protein types, after pepsin and papain hydrolysis. This was associated with the higher hydropathicity and amounts of residues associated with DPP-IV inhibition in the structural (cuticular) proteins. In silico, the peptides were mostly released with pepsin than papain. Cuticular (CP) and non-cuticular proteins (NC) were extracted from yellow mealworm and hydrolyzed with pepsin and papain in vitro to validate the virtual findings. CP hydrolysate with papain inhibited DPP-IV the most compared to CP hydrolysate with pepsin, whereas NC hydrolysates were mostly inactive. CP had higher hydrophobic–hydrophilic amino acid ratios and contents of the activity-associated residues than NC. The findings demonstrate the application of bioinformatics in processing proteins for bioactive peptide production. Practical applications: The discovery of bioactive peptides from food proteins is typically based on the classic approach involving working with a small number of protein-protease combinations in vitro. For the first time, this study reported the application of in silico tools in comprehensively studying hundreds of proteins from yellow mealworm (an edible insect) as sources of DPP-IV inhibitors, followed by in vitro processing and validation guided by the results obtained in silico. The advantage of this approach is that it allows for analysis of several protein–protease combinations (with multiple datasets of structural, functional, and bioactivity parameters) in a short time. This work is relevant in advancing research on emerging or alternative proteins as well as structure-informed food protein processing. The bioinformatics approach can be adapted for strategic processing of proteins in the food industry prior to making major resource investments.",
keywords = "bioactive peptides, bioinformatics, cuticular proteins, dipeptidyl peptidase-IV, edible insects, hydrophobicity, Tenebrio molitor",
author = "{D{\'a}valos Ter{\'a}n}, Irene and Kento Imai and Lacroix, {Isabelle M.E.} and Vincenzo Fogliano and Udenigwe, {Chibuike C.}",
year = "2019",
month = "11",
day = "28",
doi = "10.1111/jfbc.13121",
language = "English",
journal = "Journal of food biochemistry",
issn = "0145-8884",
publisher = "Wiley",

}

Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase-IV inhibitors. / Dávalos Terán, Irene; Imai, Kento; Lacroix, Isabelle M.E.; Fogliano, Vincenzo; Udenigwe, Chibuike C.

In: Journal of food biochemistry, 28.11.2019.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase-IV inhibitors

AU - Dávalos Terán, Irene

AU - Imai, Kento

AU - Lacroix, Isabelle M.E.

AU - Fogliano, Vincenzo

AU - Udenigwe, Chibuike C.

PY - 2019/11/28

Y1 - 2019/11/28

N2 - Bioinformatics was applied for strategic processing of yellow mealworm (Tenebrio molitor) proteins to produce dipeptidyl peptidase (DPP)-IV inhibiting peptides. In silico analysis of 384 mealworm proteins revealed structural proteins as better precursors of DPP-IV inhibiting peptides, compared with other protein types, after pepsin and papain hydrolysis. This was associated with the higher hydropathicity and amounts of residues associated with DPP-IV inhibition in the structural (cuticular) proteins. In silico, the peptides were mostly released with pepsin than papain. Cuticular (CP) and non-cuticular proteins (NC) were extracted from yellow mealworm and hydrolyzed with pepsin and papain in vitro to validate the virtual findings. CP hydrolysate with papain inhibited DPP-IV the most compared to CP hydrolysate with pepsin, whereas NC hydrolysates were mostly inactive. CP had higher hydrophobic–hydrophilic amino acid ratios and contents of the activity-associated residues than NC. The findings demonstrate the application of bioinformatics in processing proteins for bioactive peptide production. Practical applications: The discovery of bioactive peptides from food proteins is typically based on the classic approach involving working with a small number of protein-protease combinations in vitro. For the first time, this study reported the application of in silico tools in comprehensively studying hundreds of proteins from yellow mealworm (an edible insect) as sources of DPP-IV inhibitors, followed by in vitro processing and validation guided by the results obtained in silico. The advantage of this approach is that it allows for analysis of several protein–protease combinations (with multiple datasets of structural, functional, and bioactivity parameters) in a short time. This work is relevant in advancing research on emerging or alternative proteins as well as structure-informed food protein processing. The bioinformatics approach can be adapted for strategic processing of proteins in the food industry prior to making major resource investments.

AB - Bioinformatics was applied for strategic processing of yellow mealworm (Tenebrio molitor) proteins to produce dipeptidyl peptidase (DPP)-IV inhibiting peptides. In silico analysis of 384 mealworm proteins revealed structural proteins as better precursors of DPP-IV inhibiting peptides, compared with other protein types, after pepsin and papain hydrolysis. This was associated with the higher hydropathicity and amounts of residues associated with DPP-IV inhibition in the structural (cuticular) proteins. In silico, the peptides were mostly released with pepsin than papain. Cuticular (CP) and non-cuticular proteins (NC) were extracted from yellow mealworm and hydrolyzed with pepsin and papain in vitro to validate the virtual findings. CP hydrolysate with papain inhibited DPP-IV the most compared to CP hydrolysate with pepsin, whereas NC hydrolysates were mostly inactive. CP had higher hydrophobic–hydrophilic amino acid ratios and contents of the activity-associated residues than NC. The findings demonstrate the application of bioinformatics in processing proteins for bioactive peptide production. Practical applications: The discovery of bioactive peptides from food proteins is typically based on the classic approach involving working with a small number of protein-protease combinations in vitro. For the first time, this study reported the application of in silico tools in comprehensively studying hundreds of proteins from yellow mealworm (an edible insect) as sources of DPP-IV inhibitors, followed by in vitro processing and validation guided by the results obtained in silico. The advantage of this approach is that it allows for analysis of several protein–protease combinations (with multiple datasets of structural, functional, and bioactivity parameters) in a short time. This work is relevant in advancing research on emerging or alternative proteins as well as structure-informed food protein processing. The bioinformatics approach can be adapted for strategic processing of proteins in the food industry prior to making major resource investments.

KW - bioactive peptides

KW - bioinformatics

KW - cuticular proteins

KW - dipeptidyl peptidase-IV

KW - edible insects

KW - hydrophobicity

KW - Tenebrio molitor

U2 - 10.1111/jfbc.13121

DO - 10.1111/jfbc.13121

M3 - Article

JO - Journal of food biochemistry

JF - Journal of food biochemistry

SN - 0145-8884

M1 - e13121

ER -