Production, characterisation, and biological properties of Tenebrio molitor-derived oligopeptides.

Area of Science:

• Food Science
• Biochemistry
• Nutritional Science

Background:

• Edible insects, such as Tenebrio molitor (mealworm), are a sustainable protein source.
• Protein hydrolysates derived from Tenebrio molitor can possess bioactive properties.
• Characterization of these hydrolysates and their bioactivity is crucial for food applications.

Purpose of the Study:

• To produce and characterize protein hydrolysates from Tenebrio molitor using food-grade proteases.
• To evaluate the in vitro antioxidant and anti-inflammatory activities of these hydrolysates.
• To determine the peptidome and identify bioactive peptides for potential health benefits.

Main Methods:

• Enzymatic hydrolysis of Tenebrio molitor protein using Alcalase and Flavourzyme.
• In vitro digestion using the INFOGEST protocol.
• DPPH radical scavenging assay for antioxidant activity.
• Gene expression analysis for anti-inflammatory effects.
• Peptidome determination and in silico peptide analysis.

Main Results:

• Tenebrio molitor flour and hydrolysates demonstrated strong DPPH radical scavenging activity (EC50: 0.30–0.87 mg/mL).
• A hydrolysate produced with combined proteases reduced pro-inflammatory gene expression post-digestion.
• The complete peptidome of hydrolysates and digests was elucidated for the first time.
• Forty bioactive peptides were identified and selected for in silico evaluation.

Conclusions:

• Tenebrio molitor protein hydrolysates possess significant antioxidant and anti-inflammatory potential.
• The identified bioactive peptides warrant further investigation for functional food development.
• Edible insects represent a viable, nutritious, and sustainable food source for human consumption.