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Antioxidative Peptides from Proteolytic Hydrolysates of False Abalone (Volutharpa ampullacea perryi): Characterization, Identification, and Molecular Docking

1,2,3,†, 4,†, 2,3, 1,*, 2, 2, 2 and 1,*
School of Food Science and Technology, National Engineering Research Center of Seafood, Dalian Polytechnic University, Dalian 116034, Liaoning, China
School of Food and Biological Engineering, Engineering Research Center of Bio-process of Ministry of Education, Hefei University of Technology, Hefei 230009, Anhui, China
Anhui Province Key Laboratory of Functional Compound Seasoning, Anhui Qiangwang Seasoning Food Co., Ltd., Jieshou 236500, Anhui, China
Department of Food Science and Agricultural Chemistry, McGill University, Ste-Anne-de-Bellevue, QC H9X 3V9, Canada
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Mar. Drugs 2019, 17(2), 116;
Received: 27 December 2018 / Revised: 4 February 2019 / Accepted: 9 February 2019 / Published: 13 February 2019
(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)
PDF [3317 KB, uploaded 13 February 2019]


Antioxidative peptides were produced from false abalone (Volutharpa ampullacea perryi) using enzymatic hydrolysis. Trypsin produced the most bioactive hydrolysates with the highest scavenging ABTS+• free radicals compared to pepsin, alcalase, neutrase, and flavourzyme. The response surface methodology studies on trypsin hydrolysis indicated that the hydrolysis temperature, time, and pH were interacted with each other (p < 0.05), and the optimal conditions were hydrolysis at 51.8 °C for 4.1 h, pH 7.7 and the maximum predicted hydrolysis degree was 13.18% and ABTS+• scavenging activity of 79.42%. The optimized hydrolysate was subjected to ultrafiltration fractionation, and the fraction with MW < 3 kDa showed the highest ABTS+• scavenging activity. There were 193 peptide sequences identified from this peptide fraction and 133 of them were successfully docked onto human myeloperoxidase (MPO), an enzyme involved in forming reactive oxidants in vivo. The highest scored peptide, no. 39, consists of DTETGVPT. Its structure and molecular interactions with MPO active site were compared with previously characterized peptide hLF1-11. The interactions between peptide no. 39 and MPO include electrostatic charge, hydrogen bonds, and covalent bonds. The antioxidative peptide produced in this research may exert antioxidant activity in vivo due to its potential inhibition effect on MPO. View Full-Text
Keywords: false abalone; antioxidative peptides; ABTS+• scavenging activity; MPO; docking false abalone; antioxidative peptides; ABTS+• scavenging activity; MPO; docking

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He, S.; Zhang, Y.; Sun, H.; Du, M.; Qiu, J.; Tang, M.; Sun, X.; Zhu, B. Antioxidative Peptides from Proteolytic Hydrolysates of False Abalone (Volutharpa ampullacea perryi): Characterization, Identification, and Molecular Docking. Mar. Drugs 2019, 17, 116.

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