14C-Isotope Use to Quantify Covalent Reactions between Flavor Compounds and β-Lactoglobulin

Igor Shepelev, Gary A. Reineccius

Research output: Contribution to journalArticlepeer-review

Abstract

A 14C-based method was developed to study the rate and extent of covalent bond formation between β-lactoglobulin and three model flavor compounds: a ketone (2-undecanone UDO), an aldehyde (decanal DAL), an isothiocyanate (2-phenylethyl isothiocyanate PEITC), and an unreactive “methods blank” (decane DEC). Aqueous protein solutions with one of the 14C-labeled model flavor compounds were placed in water baths at 25, 45, and 65 °C for 4 weeks measuring the amount of flavor: protein reaction at 1, 3, 7, 14, 21, and 28 days. UDO showed lowest reactivity (max of 0.9% of added compound reacted), DAL (max of 16.4% reacted), and PEITC (max of 71.8% reacted). All compounds showed a rapid initial reaction rate which slowed after ca. 7 days. It appears that only PEITC (at 65 °C) saturated all potential protein-reactive sites over the storage period.

Original languageEnglish (US)
Pages (from-to)10579-10583
Number of pages5
JournalJournal of agricultural and food chemistry
Volume72
Issue number18
DOIs
StatePublished - May 8 2024

Bibliographical note

Publisher Copyright:
© 2024 American Chemical Society.

Keywords

  • 2-phenylethyl isothiocyanate
  • 2-undecanone
  • covalent bond
  • decanal
  • pea protein isolate

PubMed: MeSH publication types

  • Journal Article
  • Evaluation Study

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