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Modification of β–lactoglobulin by aliphatic aldehydes in aqueous solution

Published online by Cambridge University Press:  01 June 2009

Henrik Stapelfeldt  and
Leif H. Skibsted
Henrik Stapelfeldt
Affiliation:
KVL Centre for Food Research and Department of Dairy and Food Science, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark
Leif H. Skibsted*
Affiliation:
KVL Centre for Food Research and Department of Dairy and Food Science, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark
*
* For correspondance.
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Summary

Each of the secondary lipid oxidation products pentanal, hexanal and heptanal was found to react with β–lactoglobulin (β–lg) in a two-phase model System (aqueous phosphate buffer–1-octanol) yielding fluorescent condensation products (emission maximum, 410 nm; excitation maximum, 350 nm). Protein polymers were detected by size-exclusion HPLC, and the rate of reaction paralleled the formation of fluorescent products, with the reactivity being pentanal > hexanal > heptanal. Simultaneously, the reaction also changed the intrinsic fluorescence of β–lg, and in particular pentanal reduced the intensity of tryptophan fluorescence (emission maximum, 332 nm; excitation maximum, 288 nm) by 30%. These findings are discussed with reference to the effect of peroxidizing lipids on the physical properties of whey proteins and the use of protein fluorescence (induced by the reaction with aldehydes) as marker for the oxidative status of milk and whey protein products.

Type
Original Articles
Information
Journal of Dairy Research , Volume 61 , Issue 2 , May 1994 , pp. 209 - 219
Copyright
Copyright © Proprietors of Journal of Dairy Research 1994

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