Accessibility navigation

Flavor-protein binding: disulfide interchange reactions between ovalbumin and volatile disulfides

Adams, R. L., Mottram, D. S., Parker, J. K. and Brown, H. M. (2001) Flavor-protein binding: disulfide interchange reactions between ovalbumin and volatile disulfides. Journal of Agricultural and Food Chemistry, 49 (9). pp. 4333-4336. ISSN 1520-5118

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item DOI: 10.1021/jf0100797


The irreversible binding of selected sulfur-containing flavor compounds to proteins was investigated in aqueous solutions containing ovalbumin and a mixture of disulfides (diethyl, dipropyl, dibutyl, diallyl, and 2-furfuryl methyl) using solid-phase micro-extraction (SPME). In systems which had not been heated, the recovery of disulfides from the headspace above the protein at the native pH (6.7) was similar to that from an aqueous blank. However, significant losses were observed when the pH of the solution was increased to 8.0. When the protein was denatured by heating, much greater losses were observed and some free thiols were produced. In similar heat-denatured systems at pH 2.0, no losses of disulfides were observed. Disulfides containing allyl or furfuryl groups were more reactive than saturated alkyl disulfides. Interchange reactions between protein sulfhydryl groups and the disulfides are believed to be responsible for the loss of the disulfides.

Item Type:Article
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Food Research Group
ID Code:26005
Uncontrolled Keywords:Disulfides; sulfhydryl interchange; proteins; flavor binding; SPME
Publisher:American Chemical Society

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation