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        Nutraceutical effects of bioactive peptides obtained from Pterophylla beltrani (Bolivar & Bolivar) protein isolates

        Laura Jenet Montiel-Aguilar,Jorge Ariel Torres-Castillo,Rocío Rodríguez-Servin,Adiel Berenice López-Flores,Víctor Eustorgio Aguirre-Arzola,Gerardo Méndez-Zamora,Sugey Ramona Sinagawa-García 한국응용곤충학회 2020 Journal of Asia-Pacific Entomology Vol.23 No.3

        Edible insects have been important sources of food proteins for human consumption and animal feed. In this study, a protein isolate from Pterophylla beltrani Bolivar & Bolivar, 1942 (Orthoptera: Tettigoniidae) was enzymatically processed and its nutraceutical properties were evaluated. Protein isolates were obtained from an insect flour and then was hydrolyzed for 5 h with a sequential process using pepsin and trypsin-chymotrypsin to simulate the gastric intestinal fluids. To evaluate the effect of peptide molecular size on nutraceutical properties, the peptides obtained from Total hydrolyzed (TH) were fractionated by ultrafiltration (UF) with 10 kDa and 3 kDa UF membranes giving fractions (F) with different molecular size (F < 3KDa, F < 10KDa and F > 10KDa). The inhibition assay of Angiotensin-Converting Enzyme (ACE) showed that the best treatment (P < 0.05) was the (TH) with an IC50 value of 0.5 mg/mL while the F < 3KDa was the lowest (P < 0.05) with an IC50 of 1.44 mg/mL, and the peptide size had no effect. However, an α-amylase inhibition was observed with an increase of the IC50 value between TH, F > 10KDa and F < 10KDa although no significative difference (P > 0.05) was found between the TH and F < 3KDa with IC50 of 0.48 and 0.68 mg/mL, respectively. In antioxidant activity, significant differences (P < 0.05) were observed between TH and UF fractions where the best response was in the F < 3KDa. In conclusion, P. beltrani proteins isolate are a source of bioactive peptide, and these could be considered as potential edible insect and sustainable food with nutraceutical effects.

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