Multiple biological effects of secondary metabolites of Ziziphus jujuba: isolation and mechanistic insights through in vitro and in silico studies

ŞÖHRETOĞLU D., Bakir S. D., BARUT B., Soral M., SARI S.

EUROPEAN FOOD RESEARCH AND TECHNOLOGY, vol.248, no.4, pp.1059-1067, 2022 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 248 Issue: 4
  • Publication Date: 2022
  • Doi Number: 10.1007/s00217-021-03946-0
  • Journal Name: EUROPEAN FOOD RESEARCH AND TECHNOLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, ABI/INFORM, Agricultural & Environmental Science Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Compendex, Food Science & Technology Abstracts, Hospitality & Tourism Complete, Hospitality & Tourism Index, Veterinary Science Database
  • Page Numbers: pp.1059-1067
  • Keywords: Tyrosinase, alpha-Glucosidase, Jujube, Procyanidin B4, Magnoflorine, Molecular docking, MUSHROOM TYROSINASE, PROTEIN, INHIBITION, DISCOVERY, DOCKING, MODEL
  • Karadeniz Technical University Affiliated: Yes

Abstract

In this study, we tested tyrosinase and oc-glucosidase effects of different extracts of Ziziphus jujuba fruits. The n-BuOH sub-extract inhibited both tyrosinase and oc-glucosidase (IC50 =18.82 +/- 1.13 and 25.03 +/- 0.77 mu g/mL, respectively) better than the positive controls kojic acid and acarbose (IC50 =58.26 +/- 0.25 and 46.10 +/- 2.3 mu g/mL, respectively). Thus, the n-BuOH extract was selected for further phytochemical studies. Indole-3-lactic acid methylester, catechin, magnoflorine, kaempferol 3-O-alpha-rhamnopyranosyl-(1 -> 6)-beta-galactopyranoside, quercetin 3-O-alpha-rhamnopyranosyl-(1 -> 6)-beta-galactopyranoside, and procyanidin B4 were isolated from the extract. We tested alpha-glucosidase and tyrosinase inhibitory effects, as well as DNA nuclease effects of the isolated compounds. Procyanidin B4 exhibited the best activity against both tyrosinase and alpha-glucosidase (IC50 =60.25 +/- 0.88 and 170.18 +/- 5.60 mu g/mL, respectively). The isolates did not show any nuclease effect at increasing concentrations. Molecular docking studies provided insights into inhibition mechanisms of the isolates against tyrosinase and alpha-glucosidase at the molecular level.