Drivers of the In-Mouth Interaction between Lupin Protein Isolate and Selected Aroma Compounds: A Proton Transfer Reaction-Mass Spectrometry and Dynamic Time Intensity Analysis

J Agric Food Chem. 2024 Apr 17;72(15):8731-8741. doi: 10.1021/acs.jafc.3c08819. Epub 2024 Apr 5.

Abstract

Plant proteins often carry off-notes, necessitating customized aroma addition. In vitro studies revealed protein-aroma binding, limiting release during consumption. This study employs in vivo nose space proton transfer reaction-time-of-flight-mass spectrometry and dynamic sensory evaluation (time intensity) to explore in-mouth interactions. In a lupin protein-based aqueous system, a sensory evaluation of a trained "green" attribute was conducted simultaneously with aroma release of hexanal, nonanal, and 2-nonanone during consumption. Results demonstrated that enlarging aldehyde chains and relocating the keto group reduced maximum perceived intensity (Imax_R) by 71.92 and 72.25%. Protein addition decreased Imax_R by 30.91, 36.84, and 72.41%, indicating protein-aroma interactions. Sensory findings revealed a perceived intensity that was lower upon protein addition. Aroma lingering correlated with aroma compounds' volatility and hydrophobicity, with nonanal exhibiting the longest persistence. In vitro mucin addition increased aroma binding four to 12-fold. Combining PTR-ToF-MS and time intensity elucidated crucial food behavior, i.e., protein-aroma interactions, that are pivotal for food design.

Keywords: aqueous model systems; aroma compounds; binding; lupin protein; perception; proton transfer reaction of flight-mass spectrometry; release; time intensity.

MeSH terms

  • Aldehydes*
  • Mass Spectrometry / methods
  • Mouth / chemistry
  • Odorants* / analysis
  • Protons
  • Volatile Organic Compounds* / analysis

Substances

  • nonanal
  • Protons
  • Volatile Organic Compounds
  • Aldehydes