Angiotensin‐I Converting Enzyme Inhibitory and Antioxidant Activities of Egg Protein Hydrolysates Produced with Gastrointestinal and Nongastrointestinal Enzymes

Abstract

Egg is a well-known rich source of bioactive peptides. In this study, egg protein (egg white and egg yolk proteins) hydrolysates were produced with gastrointestinal enzymes (pepsin and pancreatin) or nongastrointestinal enzymes (thermolysin and alcalase), and fractionated by ultrafiltration and cation exchange chromatography. Angiotensin-I converting enzyme (ACE) inhibitory and antioxidant activities, amino acid composition and molecular weight distribution were studied, and the physicochemical properties were related with the bioactivities. Our results showed that egg protein hydrolysates produced with non-GI enzymes (thermolysin and alcalase) showed significantly higher ACE inhibitory activity, whereas similar or even lower antioxidative activities, than those of hydrolysates produced with GI enzymes. ACE-inhibitory activity significantly correlated with the amino acid composition, especially the proportion of positively charged amino acid, whereas antioxidant activities correlated with the proportion of low molecular weight peptides under 500 Da. Understanding the relationship between the bioactivities and physicochemical properties of the hydrolysates/fractions is important to facilitate the development technologies for preparing fractions with improved bioactivities.

Chemical and Cellular Antioxidant Activities of Chicken Breast Muscle Subjected to Various Thermal Treatments Followed by Simulated Gastrointestinal Digestion

“…Thus, these amino acids could contribute to ABTS activity of chicken breast digesta. You and Wu () also found that egg white and egg yolk hydrolyzed by pepsin/pancreatin showed higher antioxidant activities than those hydrolyzed by nongastrointestinal enzymes. Peptides with molecular weight less than 500 Da showed higher antioxidant activity than larger peptides (You and Wu ).…”

Purification and Identification of Antioxidant Peptides from Protein Hydrolysate of Scalloped Hammerhead (Sphyrna lewini) Cartilage

“…As shown in Figure 6A, SCPE-A, SCPE-B and SCPE-C showed dose-dependent anti-DPPH• activity, with EC 50 values of 2.43, 2.43, and 1.99 mg/mL, respectively, and SCPE-C exhibited the highest radical-scavenging activity among all samples, except the positive control of ascorbic acid. The EC 50 of SCPE-C was lower than that of Pro-Ser-Tyr-Val (PSYV) (17.0 mg/mL) [28], Thr-Thr-Ala-Asn-Ile-Glu-Asp-Arg-Arg (TTANIEDRR) (2.503 mg/mL) [26], Phe-Leu-Asn-Glu-Phe-Leu-His-Val (FLNEFLHV) (4.950 mg/mL) [29], Trp-Glu-Gly-Pro-Lys (WEGPK) (4.438 mg/mL), Gly-Val-Pro-Leu-Thr (GVPLT) (4.541 mg/mL) [5], Gly-Phe-Gly-Pro-Leu (GFGPL) (2.249 mg/mL), Val-Gly-Gly-Arg-Pro (VGGRP) (2.937 mg/mL) [30], FIMGPY (2.60 mg/mL), GPAGDY (3.48 mg/mL), IVAGPQ (3.93 mg/mL) [11], WDR(3.63 mg/mL), PYFNK (4.11 mg/mL) and LDK (3.06 mg/mL) [19,20] from the protein hydrolysates of loach, blue mussel, salmon, bluefin leatherjacket, grass carp skin, skate ( Raja porosa ) cartilage and scalloped hammerhead muscle, but it was higher than that of Gly-Ser-Gln (GSQ) (0.61 mg/mL) [31], Pro-Ile-Ile-Val-Tyr-Trp-Lys (PIIVYWK) (0.713 mg/mL), Phe-Ser-Val-Val-Pro-Ser-Pro-Lys (FSVVPSPK) (0.937 mg/mL) [29], Pro-Tyr-Ser-Phe-Lys (PYSFK) (1.575 mg/mL) [30], His-Phe-Gly-Asp-Pro-Phe-His (HFGDPFH) (0.20 mg/mL) [32], Phe-Leu-Pro-Phe (FLPF) (0.789 mg/mL), Leu-Pro-Phe (LPF) (0.777 mg/mL) and Leu-Leu-Pro-Phe (LLPF) (1.084 mg/mL) [33] from the protein hydrolysates of Chinese leek, blue mussel, grass carp skin, mussel sauce and corn gluten meal. Therefore, the present results suggested that SCPE-A, SCPE-B and SCPE-C were DPPH• inhibitors and primary antioxidants that reacted with free radicals.…”

“…The EC 50 values of SCPE-A, SCPE-B and SCPE-C were 0.28, 0.21, and 0.15 mg/mL, respectively, and SCPE-C exhibited the highest HO• scavenging activity. The EC 50 of SCPE-C was lower than that of PYFNK (0.24 mg/mL), LDK (0.17 mg/mL) [19,20], Leu-Gly-Leu-Asn-Gly-Asp-Asp-Val-Asn (LGLNGDDVN) (0.687 mg/mL) [34], PSYV (2.64 mg/mL) [28], HFGDPFH (0.50 mg/mL) [32], Phe-Pro-Glu-Leu-Leu-Ile (FPELLI) (0.57 mg/mL) and Val-Phe-Ala-Ala-Leu (VFAAL) (0.31 mg/mL) [4], as well as that of Tyr-Pro-Pro-Ala-Lys (YPPAK) (0.228 mg/mL) [23], Pro-Ser-Lys-Tyr-Glu-Pro-Phe-Val (PSKYEPFV) (2.86 mg/mL) [35], PYSFK (2.283 mg/mL), GFGPL (1.612 mg/mL), VGGRP (2.055 mg/mL) [30], Tyr-Leu-Gly-Ala-Lys (YLGAK) (scavenging rate: 45.14% at 0.5 mg/mL), Gly-Gly-Leu-Glu-Pro-Ile-Asn-Phe-Gln (GGLEPINFQ) (scavenging rate: 41.07% at 0.5 mg/mL) [36], Asn-Gly-Leu-Glu-Gly-Leu-Lys (NGLEGLK) (0.313 mg/mL), Asn-Ala-Asp-Phe-Gly-Leu-Asn-Gly-Leu-Glu-Gly-Leu-Ala (NADFGLNGLEGLA) (0.612 mg/mL) [32], FIMGPY (3.04), GPAGDY (3.92 mg/mL) and IVAGPQ (5.03 mg/mL) [11] from the protein hydrolysates of scalloped hammerhead muscle, conger eel, weatherfish loach, mussel sauce, Chinese cherry seeds, blue mussel, grass carp, egg white, giant squid and skate ( R. porosa ) cartilage. The three isolated peptides, especially SCPE-C, revealed good HO• scavenging activity, which demonstrated that it could serve as a scavenger to reduce or eliminate the damage induced by HO• in foods and biological systems.…”

Double enzyme hydrolysis for producing antioxidant peptide from egg white: Optimization, evaluation, and potential allergenicity

“…The released peptides could exhibit specific biological activities after hydrolysis, fermentation, or enzymolysis (You & Wu, 2011). The released peptides could exhibit specific biological activities after hydrolysis, fermentation, or enzymolysis (You & Wu, 2011).…”