β-Lactoglobulin as nanotransporter for allicin: Sensory properties and applicability in food

Sandra Catharina Wilde*, Julia Katharina Keppler, Kalpana Palani, Karin Schwarz

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The thiosulfinate allicin is a labile, bioactive compound of garlic. In order to enrich allicin in a functional food, a delivery system which stabilises the compound and masks its intense flavour is necessary. In the present study allicin was covalently bound to the whey protein β-lactoglobulin and the incorporation of this transporter in a food matrix was tested. The sensory properties of the pure functional ingredient as well as of an enriched beverage were characterised by quantitative descriptive analysis. The concentration of volatile compounds was analysed by headspace gas chromatography-mass spectrometry. The garlic-related organoleptic properties of garlic powder were significantly improved by the binding of allicin in combination with spray drying. After purification of the modified β-lactoglobulin the garlic taste and smell were barely perceptible. β-Lactoglobulin modified with allicin provided a stable functional ingredient that can be used to enrich a broad range of food products.

Original languageEnglish
Pages (from-to)667-674
Number of pages8
JournalFood Chemistry
Volume199
DOIs
Publication statusPublished - 15 May 2016
Externally publishedYes

Keywords

  • Allicin
  • Covalent binding
  • Functional food
  • Garlic powder
  • Sensory properties
  • Spray drying
  • Whey protein isolate
  • β-Lactoglobulin

Fingerprint

Dive into the research topics of 'β-Lactoglobulin as nanotransporter for allicin: Sensory properties and applicability in food'. Together they form a unique fingerprint.

Cite this