Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7589924 | Food Chemistry | 2016 | 8 Pages |
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.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Sandra Catharina Wilde, Julia Katharina Keppler, Kalpana Palani, Karin Schwarz,