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Open AccessArticle

Bioactive Peptides from Cartilage Protein Hydrolysate of Spotless Smoothhound and Their Antioxidant Activity In Vitro

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Zhejiang Provincial Engineering Technology Research Center of Marine Biomedical Products, School of Food and Pharmacy, Zhejiang Ocean University, 1st Haidanan Road, Changzhi Island, Lincheng, Zhoushan 316022, China
2
National and Provincial Joint Laboratory of Exploration and Utilization of Marine Aquatic Genetic Resources, National Engineering Research Center of Marine Facilities Aquaculture, School of Marine Science and Technology, Zhejiang Ocean University, 1st Haidanan Road, Changzhi Island, Lincheng, Zhoushan 316022, China
*
Authors to whom correspondence should be addressed.
Mar. Drugs 2018, 16(4), 100; https://doi.org/10.3390/md16040100
Received: 25 January 2018 / Revised: 9 March 2018 / Accepted: 10 March 2018 / Published: 22 March 2018
(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)
In the experiment, crude proteins from spotless smoothhound (Mustelus griseus), cartilages were isolated by HCl-Guanidine buffer, and its hydrolysate was prepared using trypsin at pH 8.0, 40 °C with a total enzyme dose of 2.5%. Subsequently, three antioxidant peptides were purified from the hydrolysate using membrane ultrafiltration, anion-exchange chromatography, gel filtration chromatography, and reverse phase high-performance liquid chromatography. The amino acid sequences of isolated peptides were identified as Gly-Ala-Glu-Arg-Pro (MCPE-A); Gly-Glu-Arg-Glu-Ala-Asn-Val-Met (MCPE-B); and Ala-Glu-Val-Gly (MCPE-C) with molecular weights of 528.57, 905.00, and 374.40 Da, respectively, using protein amino acid sequence analyzer and mass spectrum. MCPE-A, MCPE-B and MCPE-C exhibited good scavenging activities on 2,2-diphenyl-1-picrylhydrazyl radicals (DPPH•) (EC50 3.73, 1.87, and 2.30 mg/mL, respectively), hydroxyl radicals (HO•) (EC50 0.25, 0.34, and 0.06 mg/mL, respectively), 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid radicals (ABTS+•) (EC50 0.10, 0.05, and 0.07 mg/mL, respectively) and superoxide anion radicals ( O 2 •) (EC50 0.09, 0.33, and 0.18 mg/mL, respectively). MCPE-B showed similar inhibiting ability on lipid peroxidation with butylated hydroxytoluene (BHT) in a linoleic acid model system. Furthermore, MCPE-A, MCPE-B, and MCPE-C could protect H2O2-induced HepG2 cells from oxidative stress by decreasing the content of malonaldehyde (MDA) and increasing the levels of superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), and glutathione reductase (GSH-Rx). Glu, Gly, Met, and Pro in their sequences and low molecular weight could be attributed to the antioxidant activities of three isolated peptides. These results suggested that GAERP (MCPE-A), GEREANVM (MCPE-B), and AEVG (MCPE-C) from cartilage protein hydrolysate of spotless smoothhound might serve as potential antioxidants and be used in the pharmaceutical and health food industries. View Full-Text
Keywords: spotless smoothhound (Mustelus griseus); cartilage; protein hydrolysate; peptide; antioxidant activity; antioxidant enzyme spotless smoothhound (Mustelus griseus); cartilage; protein hydrolysate; peptide; antioxidant activity; antioxidant enzyme
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Tao, J.; Zhao, Y.-Q.; Chi, C.-F.; Wang, B. Bioactive Peptides from Cartilage Protein Hydrolysate of Spotless Smoothhound and Their Antioxidant Activity In Vitro. Mar. Drugs 2018, 16, 100.

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