Highlights

• This study introduces an innovative technique that combines MCX-SPE, LC-MS, and FBMN to efficiently identify bioactive peptides from Bifidobacterium.
• This technique could identify twenty-five novel peptides from Bifidobacterium cultures, highlighting the method’s effectiveness in discovering and characterizing peptides.
• One of the peptides discovered showed a significant ACE inhibitory activity, underscoring the potential therapeutic applications of the findings.

Summary

This research introduces a novel method to identify bioactive peptides from probiotics, focusing on three strains of Bifidobacterium. Utilizing a combination of mixed-mode cationic exchange based solid-phase extraction (MCX-SPE), liquid chromatography-mass spectrometry (LC–MS), and feature-based molecular networking (FBMN), the study successfully identified twenty-five new peptides. Notably, this included peptides uniquely produced by B. animalis under specific treatments, with one demonstrating significant angiotensin-converting-enzyme (ACE) inhibitory effects.

Bifidobacterium, commonly found in the human gut and dairy products, produces bioactive peptides with health benefits, including antimicrobial and antioxidant effects. Traditional methods of identifying these peptides face challenges like interference from other compounds and low peptide concentrations.

The integrated approach adopted in this research simplifies sample preparation and leverages advanced techniques to improve these peptides’ detection, characterization, and analysis, facilitating faster development of functional foods and nutraceuticals. This efficient, cost-effective method underscores the peptides’ importance in health promotion and disease prevention.

S. Chen et al., “Discovery of the bioactive peptides secreted by Bifidobacterium using integrated MCX coupled with LC–MS and feature-based molecular networking,” Food Chemistry, vol. 347, p. 129008, Jun. 2021, doi: 10.1016/j.foodchem.2021.129008.