W.H. (Walter) Heijnis: Enzymatic cross-linking of the milk protein α lactalbumin

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10 Dec 2010 16:00
Location: Aula, building 362, Gen. Foulkesweg 1, Wageningen
Organisation: Wageningen University
Promotor: prof.dr.ir. H. Gruppen (Food Chemistry)
Promotor: dr. W.J.H. van Berkel
Co Promotor: dr.ir. P.A. Wierenga

The cross-linking of proteins results in a change in the specific structure of a protein. These structural changes result in different behavior of the protein in food. This research focused on the cross-linking of the milk protein α lactalbumin … the enzyme peroxidase. Theoretically, this protein can form cross-links at multiple places which result in the formation of many different new protein structures. Each of these protein structures having their own behavior. Directing of the cross-linking reaction was the main theme of the research to decrease the number of protein structures formed. The specific site of cross-linking was an important part of the research. Cross-linked α lactalbumin shows a decreased formation of foam in comparison to the starting protein. Therefore the cross-linked α lactalbumin can be used as an anti-foam in foods.


Title thesis:   Peroxidase-mediated cross linking of bovine α lactalbumin

More information:
» Enzymatic crosslinking of food proteins (pdf)
» Process on a Chip (website nwo)

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