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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

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To link to this article DOI: 10.1021/jf0100797

Abstract/Summary

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

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