Identification and characterization of angiotensin-converting enzyme inhibitory peptide from bovine bone

  • YANG Zeyao ,
  • XU Jing ,
  • WANG Jiangxue ,
  • WANG Ziye ,
  • XI Fanwei ,
  • CAO Songmin
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  • (School of Food Science and Engineering, Ningxia University, Yinchuan 750021, China)

Received date: 2024-08-13

  Revised date: 2024-10-17

  Online published: 2025-08-04

Abstract

Animal bones, as the main by-product of the meat industry, have not been fully utilized and possess low added value.In this study, bovine bone was used as the raw material to prepare a bovine bone hydrolysate with high angiotensin-converting enzyme (ACE) inhibitory activity using controllable enzymatic hydrolysis technology.The highly active ACE inhibitory peptide was then isolated, purified, and identified using multi-column tandem chromatography and Nano-LC-ESI-MS/MS technology.Finally, the bovine bone peptide (Gly-Phe-Ser-Gly-Phe-Arg,GPSGPR) (IC50=382.16 μmol/L) with high ACE inhibitory activity was identified.Molecular simulation docking results showed that the amino acid residues in GPSGPR mainly exert the inhibitory effect on ACE by forming stable hydrogen bonds with the active sites in the three active pockets of ACE.The results of rat serum enzyme resistance experiments demonstrated that GPSGPR exhibits high enzyme resistance in rat plasma, maintaining 50.01% integrity after 6 hours of in vitro cultivation.The results of this study indicate that bovine bone has high potential in the preparation of ACE inhibitory peptides, offering a valuable reference for the high-value utilization of by-products in animal product processing.

Cite this article

YANG Zeyao , XU Jing , WANG Jiangxue , WANG Ziye , XI Fanwei , CAO Songmin . Identification and characterization of angiotensin-converting enzyme inhibitory peptide from bovine bone[J]. Food and Fermentation Industries, 2025 , 51(13) : 234 -242 . DOI: 10.13995/j.cnki.11-1802/ts.040739

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