Production of Protein Hydrolysates with Antioxidant and Antihypertensive Activity from Edible Larvae of Aegiale hesperiaris and Comadia redtenbacheri

Abstract

The search for sustainable and health-promoting food sources has increased interest in edible insects, which are rich in proteins and bioactive compounds with potential nutraceutical applications. In this study, we evaluated the bioactive properties of protein hydrolysates derived from Aegiale hesperiaris (maguey white worm, WW) and Comadia redtenbacheri (maguey red worm, RW), two culturally and economically significant insect species in Mexico. Hydrolysates were obtained via enzymatic treatments: either single hydrolysis with pepsin (PH) or sequential hydrolysis with pepsin followed by trypsin (PTH). The PTH hydrolysates exhibited strong antioxidant activity, with 2,2-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical inhibition above 90% and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging capacity between 75-85%. Additionally, they showed significant angiotensin-converting enzyme (ACE) inhibitory activity, reaching IC₅₀ values of 0.35 and 0.017 μg/mL for WWPH and RWPH, respectively-the latter outperforming the commercial drug Enalapril (IC₅₀ = 0.11 μg/mL). SDS-PAGE analysis revealed low molecular weight peptides (<10 kDa), especially between 5-9 kDa, associated with enhanced bioactivity. Peptides from RW also showed low Hill coefficients, suggesting a gradual and sustained interaction with ACE. These findings support the use of insect-derived hydrolysates as promising multifunctional ingredients for the development of functional foods targeting cardiovascular health.

Keywords: Aegiale hesperiaris; Comadia redtenbacheri; angiotensin- converting enzyme (ACE) inhibitory activity; antioxidant activity; bioactive peptides; bioactive properties; edible insects; enzymatic hydrolysis.

Figure 1

SDS-PAGE patterns of Aegiale hesperiaris and Comadia redtenbacheri concentrates and hydrolysates. MWM: molecular weight marker; WWPC: Aegiale hesperiaris protein concentrate; WWPH: single hydrolysis (pepsin) of Aegiale hesperiaris extracts; WWPTH: sequential hydrolysis (pepsin-trypsin) of Aegiale hesperiaris extracts; RWPC: Comadia redtenbacheri protein concentrate; RWPH: single hydrolysis (pepsin) of Comadia redtenbacheri extracts; RWPTH: sequential hydrolysis (pepsin-trypsin) of Comadia redtenbacheri extracts.

Figure 2

Antioxidant activity of protein concentrates and hydrolysates of Aegiale hesperiaris (WW) and Comadia redtenbacheri (RW). WWPC: Aegiale hesperiaris protein concentrate; WWPH: single hydrolysis (pepsin) of Aegiale hesperiaris extracts; WWPTH: sequential hydrolysis (pepsin-trypsin) of Aegiale hesperiaris extracts; RWPC: Comadia redtenbacheri protein concentrate; RWPH: single hydrolysis (pepsin) of Comadia redtenbacheri extracts; RWPTH: sequential hydrolysis (pepsin-trypsin) of Comadia redtenbacheri extracts. Different letters (a–f) between samples indicate significant differences (p < 0.05). Results are shown as mean ± standard deviation (n = 3).

Figure 3

ACE inhibition of protein concentrates and hydrolysates from Aegiale hesperiaris and Comadia redtenbacheri. Values are expressed as mean ± SD of duplicate assays. The statistical difference (p < 0.05) with respect to the two species in their different treatments and the commercial inhibitor (Enalapril, control +) is presented with the letters a–e.

Figure 4

Mechanisms of enzyme inhibition comparing the action of the commercial inhibitor (Enalapril) and the hydrolysates of Aegiale hesperiaris and Comadia redtenbacheri on ACE, according to the Hill coefficient “n” and the type of inhibition.