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Studies on Enzymatic Crosslinking of Casein Micelles

Author

Listed:
  • C. Partschefeld
  • J. Schreiner

    (Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: claudia.partschefeld@chemie.tu-dresden.de)

  • U. Schwarzenbolz

    (Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: claudia.partschefeld@chemie.tu-dresden.de)

  • T. Henle

    (Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: claudia.partschefeld@chemie.tu-dresden.de)

Abstract

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.

Suggested Citation

  • C. Partschefeld & J. Schreiner & U. Schwarzenbolz & T. Henle, 2009. "Studies on Enzymatic Crosslinking of Casein Micelles," Czech Journal of Food Sciences, Czech Academy of Agricultural Sciences, vol. 27(SpecialIs), pages 99-101.
    • Handle: RePEc:caa:jnlcjf:v:27:y:2009:i:specialissue1:id:938-cjfs
    DOI: 10.17221/938-CJFS
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