sRAGE-binding and antimicrobial bioactivities of soy and pea protein after heating and in vitro infant digestion

Jiaying Tang, Malgorzata Teodorowicz, Sjef Boeren, Harry J. Wichers, Kasper A. Hettinga*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

During infant formula production, proteins are always heated, potentially affecting their digestibility and the bioactivities of resulting peptides. Although plant proteins are a promising dairy alternative for infant formula, they remain understudied, necessitating further investigations. Therefore, this research aimed to fill this gap by assessing the impact of different heating modes on soy protein (SP) and pea protein (PP), focusing on glycation levels, peptide formation during in vitro infant digestion, and immune protection potential (sRAGE-binding and antimicrobial activities) of the resulting peptides. Consequently, dry heating led to increased glycation and glycated peptide production, particularly with higher glycation in PP than SP. Moreover, PP exhibited an overall stronger sRAGE-binding capacity than SP, regardless of heating and digestion conditions. Regarding antimicrobial activity, both SP and PP-derived peptides displayed reduced effectiveness against Enterobacter cloacae after dry heating. Additionally, Staphylococcus epidermidis was differently inhibited, where PP-derived peptides showed inherent inhibition. The primary determinant of sRAGE-binding and antimicrobial potential in digestion-derived peptides was the protein source. Subsequent bioinformatics analysis predicted 519 and 133 potential antimicrobial peptides in SP and PP, respectively. This study emphasises the importance of protein source for infant formula to ensure infant health.

Original languageEnglish
Article number114224
JournalFood Research International
Volume183
DOIs
Publication statusPublished - May 2024

Keywords

  • Antimicrobial
  • Bioinformatics
  • Glycation
  • Heating
  • Immune protection
  • Peptidomics
  • Plant protein
  • sRAGE

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