European Food Research and Technology

, Volume 245, Issue 3, pp 677–689 | Cite as

Bioactive peptide with antioxidant and anticancer activities from black soybean [Glycine max (L.) Merr.] byproduct: isolation, identification and molecular docking study

  • Zhongqin Chen
  • Weiwei Li
  • Ramesh Kumar Santhanam
  • Cong Wang
  • Xudong Gao
  • Yue Chen
  • Chunli Wang
  • Leilei Xu
  • Haixia ChenEmail author
Original Paper


In this study, a novel peptide was isolated from the black soybean byproduct using bioactive guided isolation technique. Initially, the hydrolysate of black soybean protein was fractionated and separated sequentially by ultrafiltration, Sephadex G 25 chromatography and reverse-phase HPLC techniques. The peptide fractions that collected in each step were tested for their antioxidant capacity and anticancer activities against human liver (HepG2), lung (MCF-7) and cervical (Hela) cancer cell lines. The most active fraction was subjected to further purification. The final purified peptide fraction (F2-c) with the molecular weight of 455.0 Da showed highest DPPH free radical scavenging and hydroxyl radical scavenging activity with the IC50 values of 0.12 and 0.037 µM, respectively. Moreover, it showed high cytotoxic potential against HepG2, MCF-7 and Hela cells with the IC50 values of 0.22, 0.15 and 0.32 µM, respectively. The amino acid sequence of F2-c was identified as Leu/Ile-Val-Pro-Lys (L/I-VPK). Molecular docking studies revealed that the purified peptides effectively bound with four apoptosis related key proteins (XIAP, caspase-3, caspase-7, and Bcl-2) via hydrophobic effects and hydrogen bonds, amongst them, the peptide-caspase-3 binding showed the strongest binding energy. All the results suggested that the peptide fraction Leu/Ile-Val-Pro-Lys from black soybean byproduct with significant antioxidant and anticancer activities could be a good candidate for functional foods or related drugs.

Graphical abstract


Black soybean byproduct Purification of peptide Antioxidant activity Anticancer activity Amino acid sequence Molecular docking 



This work was supported by the Grant from National High Technology Research and Development Program (“863"Program) of China (Grant no. SS2013AA100207) and the National Natural Science Foundation of China (NSFC 31371879).

Compliance with ethical standards

Conflict of interest

There are no conflicts of interest to declare.

Compliance with ethics requirements

This article does not contain any studies with human or animal subjects.

Supplementary material

217_2018_3190_MOESM1_ESM.docx (162 kb)
Supplementary material 1 (DOCX 161 KB)


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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Zhongqin Chen
    • 1
  • Weiwei Li
    • 1
  • Ramesh Kumar Santhanam
    • 1
  • Cong Wang
    • 1
  • Xudong Gao
    • 1
  • Yue Chen
    • 1
  • Chunli Wang
    • 1
  • Leilei Xu
    • 1
  • Haixia Chen
    • 1
    Email author
  1. 1.Tianjin Key Laboratory for Modern Drug Delivery and High-Efficiency, School of Pharmaceutical Science and TechnologyTianjin UniversityTianjinPeople’s Republic of China

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