FOOD SCIENCE ›› 2023, Vol. 44 ›› Issue (24): 155-163.doi: 10.7506/spkx1002-6630-20230302-021

• Bioengineering • Previous Articles     Next Articles

Isolation, Purification, Identification and Hypolipidemic Activity of Lipase Inhibitory Peptide from Chlorella pyrenoidosa

LIN Luan, LIU Wenjun, HUANG Junyuan, JIA Aijing, WANG Dengmi, LIU Bin, ZHAO Chao   

  1. (1. College of Food Science, Fujian Agricultural and Forestry University, Fuzhou 350002, China;2. College of Oceanology and Food Science, Quanzhou Normal University, Quanzhou 362000, China;3. Fujian Province Key Laboratory for the Development of Bioactive Material from Marine Algae, Quanzhou 362000, China)
  • Online:2023-12-25 Published:2024-01-02

Abstract: In this study, pancrelipase inhibitory peptides (PES) from an enzymatic protein hydrolysate of Chlorella pyrenoidosa were isolated and purified by ultrafiltration and Sephadex gel chromatography. The in vivo hypolipidemic activity of PES was evaluated by fat deposition and the levels of triglyceride (TG) and total cholesterol (TC) in Caenorhabditis elegans fed a high sugar diet. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to identify the peptide sequence of PES, and molecular docking was used to select potential pancreatic lipase inhibitory peptides, and the pancreatic lipase inhibitory activity of the synthesized peptides was verified. The results showed that PES had good hypolipidemic activity at a concentration of 1 mg/mL; it inhibited lipid deposition by 22.5%, and reduced the levels of TG and TC by 27.4% and 29.4%, respectively. In total, 999 peptides were identified, and four potential lipase inhibitory peptides were obtained. Among them, FLGPF had the best inhibitory effect on pancreatic lipase, with an inhibition rate of 50.12% at 8 mg/mL. The inhibition was reversible and non-competitive, with an inhibition constant of 5.23 mg/mL. Molecular docking showed that FLGPF could better bind to human pancreatic triacylglycerol lipase (PTL) via π-hydrogen, π-cation and hydrogen bond interactions. This study can provide a theoretical reference for the development and utilization of C. pyrenoidosa protein-derived hypolipidemic peptide.

Key words: Chlorella pyrenoidosa; lipase inhibitory peptide; Caenorhabditis elegans; hypolipidemic; molecular docking; inhibitory kinetics

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