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. S U PP O RTI N G I N FO R M ATI O NAdditional supporting information may be found online in the Supporting Information section.How to cite this article: Dávalos Terán I, Imai K, Lacroix IME, Fogliano V, Udenigwe CC. Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase-IV inhibitors. J Food Biochem. 2020;44:e13121. https ://doi.

Evaluation of Tenebrio molitor protein as a source of peptides for modulating physiological processes

“…66 To the best of our knowledge, only high DPP-IV inhibitory peptides from cuticular protein from T. molitor hydrolysed with papain (IC 50 of 0.82 mg mL −1 ) have been identified. 25 Hence, this is the first study describing the in vitro antidiabetic activity of Tenebrio molitor hydrolysates obtained from assay of a set of commercial proteases.…”

“…To our knowledge, little on the in vitro DPP-IV inhibitory properties of T. molitor protein or derived hydrolysates has been reported so far. 25 The aim of this work is to explore the in vitro ACE inhibitory, antioxidant capacity and DPP-IV inhibitory activities of Tenebrio molitor hydrolysates obtained by a set of conventional and combined enzymatic treatments employing commercial food-grade proteases (i.e. subtilisin, trypsin, ficin and flavourzyme), by studying the influence of both enzymatic treatment and degree of hydrolysis on the in vitro activities.…”

Machine learning screening of bile acid-binding peptides in a peptide database derived from food proteins

“…In addition, it implements predictive tools, including the theoretical degree of hydrolysis and bioactivity prediction. Using the BIOPEP-UWM database, the appropriate fraction of DPP-4 (dipeptidyl peptidase-4) inhibiting peptides derived from mealworms ( Tenebrio molitor ) was selected 12 . This approach has also been adopted in pigeon pea ( Cajanus cajan ) 13 .…”

In Silico Screening of a Bile Acid Micelle Disruption Peptide for Oral Consumptions from Edible Peptide Database

“…For instance, the binding affinity with target molecules is calculated by bioinformatics using the physicochemical properties of peptides. In a recent study, to select the most effective method to identify and recover dipeptidyl peptidase-4 (EC 3.4.14.5) inhibiting peptides from mealworm (Tenebrio molitor), Uniprot and BIOPEP enzyme action tools, ExPASy, were used [6]. In order to identify and recover the antioxidant peptides from flaxseed proteins effectively, informatics tools such as ExPASy and the 'Peptides' package in R were used [7].…”