Studies on Enzymatic Crosslinking of Casein Micelles

The aim of our study was to gain insights into the reactions occurring in casein micelles during enzymatic modification with microbial transglutaminase (mTG). Therefore, UHT-treated milk was incubated with varying amounts of mTG and the caseins were analysed using different analytical methods. Regarding the casein species, it was observed that β -casein was crosslinked to a higher extent than the α-caseins. From this it can be suggested that β-casein is mainly located in the outer space of the micellar structure and therefore better accessible to mTG than α-caseins, which are located predominantly in the interior. Furthermore, it was demonstrated by gel-permeation chromatography and RP-HPLC that the caseins are fixed within the micellar structure, by what the ratio of extramicellar casein decreased. We conclude that an isopeptide network in the outer β -casein rich "shell" of the micelle is formed by mTG, which is responsible for the increased micellar stability.

Abstract licence: CC BY-NC

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