Identification of angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of pork loin

Abstract

This study aimed to identify angiotensin I-converting enzyme (ACE) inhibitory peptides in enzymatic hydrolysates from pork loin. Pork hydrolysates were produced by injecting different enzymes to the loins as follows: un-injected pork (fresh pork), injected with water (no enzyme control), 100 ppm protease type XIII (E1), 80 ppm thermolysin (E2), and the combination of 100 ppm protease type XIII and 80 ppm thermolysin (E3). The highest degree of hydrolysis (96.7%) and ACE inhibitory activity (90.1%) were observed in the E2-treated hydrolysate. Next, the E2-treated hydrolysate was fractionated and purified by using two different chromatographic methods, and the fractions with the highest ACE inhibitory activity were selected at each step. Finally, two peptides (Leu-Val-Gly-Arg-Pro-Arg-His-Gly-Gln and Val-Phe-Pro-Ser) were identified in the E2treated hydrolysate using UPLC-QTOF-MS/MS. The smaller peptide, Val-Phe-Pro-Ser, showed a lower IC 50 value for ACE inhibitory activity than the nona-peptide and captopril, a commercial ACE inhibitor. The results of this study suggest that the isolated nona-peptide, Leu-Val-Gly-Arg-Pro-Arg-His-Gly-Gln, possessed strong ACE inhibitory activity. Therefore, overnight incubation of fresh pork in a refrigerator after thermolysin injection may make the pork more beneficial for human consumption.

In Silico Identification of Peptides with PPARγ Antagonism in Protein Hydrolysate from Rice (Oryza sativa)

“…All the peptides analyzed present amino acids with hydrophobic lateral chains. In silico, in vitro, and in vivo studies have reported that molecules that present nonpolar and hydrophobic amino acids (VAL, LYS, ILE, ALA, TRP, MET, PRO, and, especially, PHE) are crucial for their functionality as bioactive compounds for hydrophobic interactions [ 14 , 40 , 41 ].…”

Protein Concentrates on Tepary Bean (Phaseolus acutifolius Gray) as a Functional Ingredient: In silico Docking of Tepary Bean Lectin to Peroxisome Proliferator-Activated Receptor Gamma

“…The molecules GW9662 and G3335, which are widely known for their antiadipogenic effect via PPARγ (55,56), showed the formation of hydrogen bonds to Ser289 and Cys285 for GW9662 and Tyr473, Met364, His323, and Ser289 for G3335, with binding energies of −7.98 and −5.64 kcal/mol, respectively, for which the TTPW and ITY peptides are the ones that could present this antiadipogenic effect taking as reference the energies and binding sites of the controls used. Also, it is essential to consider the presence of hydrophobic amino acids (V, L, I, A, F, W, M, and P) since it has been reported that hydrophobic interactions is crucial for their functionality as bioactive compounds (57,58). Oseguera Toledo et al (59) have reported that the peptides FFL, LLSL, and LVLL, with a high content of hydrophobic amino acids, present a 13-28% inhibition in lipid accumulation.…”