2. Purification and Identification of Antioxidant Peptides from Protein Hydrolysate of Scalloped Hammerhead (Sphyrna lewini) Cartilage
Xue-Rong Li, Chang-Feng Chi, Li Li, Bin Wang Mar Drugs. 2017 Mar 1;15(3):61. doi: 10.3390/md15030061.
The aim of this study was to purify and identify peptides with antioxidant properties from protein hydrolysate of scalloped hammerhead (Sphyrna lewini) cartilage. Cartilaginous proteins of the scalloped hammerhead were extracted by guanidine hydrochloride, and three antioxidant peptides, named enzymolysis peptide of scalloped hammerhead cartilage A (SCPE-A), SCPE-B and SCPE-C, were subsequently isolated from the hydrolysate of the cartilaginous proteins using ultrafiltration and chromatography. The amino acid sequences of SCPE-A, SCPE-B and SCPE-C were identified as Gly-Pro-Glu (GPE), Gly-Ala-Arg-Gly-Pro-Gln (GARGPQ), and Gly-Phe-Thr-Gly-Pro-Pro-Gly-Phe-Asn-Gly (GFTGPPGFNG), with molecular weights of 301.30 Da, 584.64 Da and 950.03 Da, respectively. As per in vitro activity testing, SCPE-A, SCPE-B and SCPE-C exhibited strong scavenging activities on 2,2-diphenyl-1-picrylhydrazyl radicals (DPPH·) (half elimination ratio (EC50) 2.43, 2.66 and 1.99 mg/mL), hydroxyl radicals (HO·) (EC50 0.28, 0.21 and 0.15 mg/mL), 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid radicals (ABTS⁺·) (EC50 0.24, 0.18 and 0.29 mg/mL), and superoxide anion radicals ( O 2 - ·) (EC50 0.10, 0.14 and 0.11 mg/mL). In addition, SCPE-A showed inhibition activity similar to butylated hydroxytoluene (BHT) in lipid peroxidation in a linoleic acid model system. The amino acid residues of Gly, Pro and Phe could positively influence the antioxidant activities of GPE, GARGPQ and GFTGPPGFNG. These results suggested that GPE, GARGPQ and GFTGPPGFNG might serve as potential antioxidants and be used as food additives and functional foods.
3. Protein digestomic analysis reveals the bioactivity of deer antler velvet in simulated gastrointestinal digestion
Yang Yu, Yan Jin, Fangjun Wang, Jiaze Yan, Yanxia Qi, Mingliang Ye Food Res Int. 2017 Jun;96:182-190. doi: 10.1016/j.foodres.2017.04.002. Epub 2017 Apr 5.
Proteins are the most prominent bioactive component in deer antler velvet. The aim of the present study was to track the fate of protein of antler velvet by protein digestomics. The peptide profile identified by LC-MS/MS and the in vitro bioactivity of antler velvet aqueous extract (AAE) were investigated in simulated gastrointestinal digestion. A total of 23, 387 and 417 peptides in AAE, gastric and pancreatic digests were identified using LC-MS/MS, respectively. Collagens, the predominant proteins, released 34 peptides in gastric digests and 146 peptides in pancreatic digests. The gastric and pancreatic digests presented dipeptidyl peptidase IV (DPP-IV) and prolyl endopeptidase (PEP) inhibition activities. Four peptides from digests were proved to be DPP-IV and PEP inhibitory peptides. The results showed that the peptides released from antler velvet protein contributed to the bioactivity of antler velvet during digestion.
